Jump to content

Biotin carboxyl carrier protein: Difference between revisions

Add links
From Wikipedia, the free encyclopedia
Browse history interactively
← Previous editNext edit →
Content deleted Content added
VisualWikitext
Trivas47 (talk | contribs)
19 edits
No edit summary
Trivas47 (talk | contribs)
19 edits
added information on structure with citations
Tags: nowiki added Visual edit
Line 2: Line 2:
{{Unreferenced|date=December 2009}}
{{Unreferenced|date=December 2009}}
[[File:BCCP.png|thumb| '''Biotin Carboxyl Carrier Protein''']]
[[File:BCCP.png|thumb| '''Biotin Carboxyl Carrier Protein''']]
'''Biotin Carboxyl Carrier Protein''' (BCCP) refers to proteins containing a [[biotin attachment domain]] that carry [[biotin]] and carboxybiotin throughout the [[Adenosine triphosphate|ATP]]-dependent carboxylation by biotin-dependent carboxylases. The biotin carboxyl carrier protein is an Acetyl CoA subunit that allows for Acetyl CoA to be catalyzed and converted to malonyl-CoA. More specifically, BCCP catalyzes the carboxylation of the carrier protein to form an intermediate. Then the carboxyl group is transferred by the transcacrboxylase to form the malonyl-CoA[https://www.uniprot.org/uniprotkb/Q42533/entry .] This conversion is an essential step in the biosynthesis of fatty acids. In the case of ''[[E. coli]]'' [[Acetyl-CoA carboxylase]], the BCCP is a separate protein known as ''accB'' ({{UniProt|P0ABD8}}). On the other hand, in ''[[Haloferax mediterranei]]'' [[Propionyl-CoA carboxylase]], the BCCP ''pccA'' ({{UniProt|I3R7G3}}) is fused with [[biotin carboxylase]].
'''Biotin Carboxyl Carrier Protein''' (BCCP) refers to proteins containing a [[biotin attachment domain]] that carry [[biotin]] and carboxybiotin throughout the [[Adenosine triphosphate|ATP]]-dependent carboxylation by biotin-dependent carboxylases. The biotin carboxyl carrier protein is an Acetyl CoA subunit that allows for Acetyl CoA to be catalyzed and converted to malonyl-CoA. More specifically, BCCP catalyzes the carboxylation of the carrier protein to form an intermediate. Then the carboxyl group is transferred by the transcacrboxylase to form the malonyl-CoA.<ref>{{Cite web |title=UniProt |url=https://www.uniprot.org/uniprotkb/Q42533/entry |access-date=2023-04-26 |website=www.uniprot.org}}</ref> This conversion is an essential step in the biosynthesis of fatty acids. In the case of ''[[E. coli]]'' [[Acetyl-CoA carboxylase]], the BCCP is a separate protein known as ''accB'' ({{UniProt|P0ABD8}}). On the other hand, in ''[[Haloferax mediterranei]]'' [[Propionyl-CoA carboxylase]], the BCCP ''pccA'' ({{UniProt|I3R7G3}}) is fused with [[biotin carboxylase]].


The biosynthesis of fatty acids in plants, such as [[Triglyceride|triacylglycerol]], is vital to the plant's overall health because it allows for accumulation of seed oil. The biosynthesis that is catalyzed by BCCP usually takes place in the chloroplast of plant cells. The biosynthesis performed by the BCCP protein allows for the transfer of CO<sub>2</sub> within active sites of the cell[https://www.ebi.ac.uk/interpro/entry/InterPro/IPR001249/ .]
The biosynthesis of fatty acids in plants, such as [[Triglyceride|triacylglycerol]], is vital to the plant's overall health because it allows for accumulation of seed oil. The biosynthesis that is catalyzed by BCCP usually takes place in the chloroplast of plant cells. The biosynthesis performed by the BCCP protein allows for the transfer of CO<sub>2</sub> within active sites of the cell.<ref>{{Cite web |title=InterPro |url=https://www.ebi.ac.uk/interpro/entry/InterPro/IPR001249/ |access-date=2023-04-26 |website=www.ebi.ac.uk}}</ref>


The biotin carboxyl carrier protein carries approximately 1 mol of biotin per 22,000 g of protein[https://www.pnas.org/doi/10.1073/pnas.68.7.1512 .]
The biotin carboxyl carrier protein carries approximately 1 mol of biotin per 22,000 g of protein.<ref>{{Cite journal |last=Fall |first=R. Ray |last2=Nervi |first2=A. M. |last3=Alberts |first3=Alfred W. |last4=Vagelos |first4=P. Roy |date=1971-07 |title=Acetyl CoA Carboxylase: Isolation and Characterization of Native Biotin Carboxyl Carrier Protein |url=https://pnas.org/doi/full/10.1073/pnas.68.7.1512 |journal=Proceedings of the National Academy of Sciences |language=en |volume=68 |issue=7 |pages=1512–1515 |doi=10.1073/pnas.68.7.1512 |issn=0027-8424 |pmc=PMC389229 |pmid=4934522}}</ref>


There is not much research on BCCPs at the moment. However, a recent [https://bmcgenomics.biomedcentral.com/articles/10.1186/s12864-022-08920-y#:~:text=Biotin%20carboxyl%20carrier%20protein%20(BCCP,novo%20biosynthesis%20of%20fatty%20acids. study]
There is not much research on BCCPs at the moment. However, a recent [https://bmcgenomics.biomedcentral.com/articles/10.1186/s12864-022-08920-y#:~:text=Biotin%20carboxyl%20carrier%20protein%20(BCCP,novo%20biosynthesis%20of%20fatty%20acids. study]<ref>{{Cite journal |last=Megha |first=Swati |last2=Wang |first2=Zhengping |last3=Kav |first3=Nat N. V. |last4=Rahman |first4=Habibur |date=2022-10-17 |title=Genome-wide identification of biotin carboxyl carrier subunits of acetyl-CoA carboxylase in Brassica and their role in stress tolerance in oilseed Brassica napus |url=https://doi.org/10.1186/s12864-022-08920-y |journal=BMC Genomics |volume=23 |issue=1 |pages=707 |doi=10.1186/s12864-022-08920-y |issn=1471-2164}}</ref>
<references group="BMC Genomics" />
<references group="https://bmcgenomics.biomedcentral.com/articles/10.1186/s12864-022-08920-y#:~:text=Biotin%20carboxyl%20carrier%20protein%20(BCCP,novo%20biosynthesis%20of%20fatty%20acids." />
on plant genomics found that ''Brassica'' BCCPs might play a key role in abiotic and biotic stress responses. Meaning that these proteins may be relaying messages to the rest of the plant body after it has been exposed to extreme conditions that disrupt the plant's homeostasis.
on plant genomics found that ''Brassica'' BCCPs might play a key role in abiotic and biotic stress responses. Meaning that these proteins may be relaying messages to the rest of the plant body after it has been exposed to extreme conditions that disrupt the plant's homeostasis.

'''Structure'''

The first report of the BCCP structure was made by biochemists F. K. Athappilly and W. A. Hendrickson in 1995.<ref>{{Cite journal |last=Athappilly |first=F. K. |last2=Hendrickson |first2=W. A. |date=1995-12-15 |title=Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing |url=https://pubmed.ncbi.nlm.nih.gov/8747466/ |journal=Structure (London, England: 1993) |volume=3 |issue=12 |pages=1407–1419 |doi=10.1016/s0969-2126(01)00277-5 |issn=0969-2126 |pmid=8747466}}</ref> It can be thought of as a long β-hairpin structure, with four pairs of antiparallel β-strands that wrap around a central hydrophobic core. The biotinylation motif Met-Lys-Met is located at the tip of the β-hairpin structure. Rotations around the CαCβ bond of this Lys residue contribute to the swinging-arm model. The connection to the rest of the enzyme at the N-terminus of BCCP core is located at the opposite end of the structure from the biotin moiety. Rotations around this region contribute to the swinging-domain model, and the N1′ atom of biotin is ~ 40 Å from this pivot point. This gives a range of ~ 80 Å for the swinging-domain model, and the BC–CT active site distances observed so far are between 40 and 80 Å.<ref>Chareeporn Akekawatchai, Sarawut Jitrapakdee,

Chapter Twelve - Cellular signals integrate cell cycle and metabolic control in cancer,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 397-423,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2023.01.002</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162323000020</nowiki>)

Keywords: Cancer; Growth factors; Receptor tyrosine kinase; Cell cycle; Metabolism; Apoptosis

Debarun Patra, Kumari Bhavya, Palla Ramprasad, Moyna Kalia, Durba Pal,

Chapter Eleven - Anti-cancer drug molecules targeting cancer cell cycle and proliferation,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 343-395,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2022.11.011</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162322001006</nowiki>)

Keywords: Cancer cells; Cell cycle; Cell proliferation; Targeted therapy; Checkpoint inhibitors

Mamta Panda, Elora Kalita, Abhishek Rao, Vijay Kumar Prajapati,

Chapter Fourteen - Mechanism of cell cycle regulation and cell proliferation during human viral infection,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 497-525,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2022.11.013</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S187616232200102X</nowiki>)

Keywords: Cell cycle; Viral regulation; Immune checkpoints; DNA viruses; RNA viruses; Host pathogen interaction

Esra Albayrak, Fatih Kocabaş,

Chapter Thirteen - Therapeutic targeting and HSC proliferation by small molecules and biologicals,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 425-496,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2022.11.012</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162322001018</nowiki>)

Keywords: Hematopoietic stem cells; Small molecule; Ex vivo expansion; HSC transplantation

Leena Arora, Moyna Kalia, Durba Pal,

Chapter Nine - Role of macrophages in cancer progression and targeted immunotherapies,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 281-311,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2022.11.010</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162322000992</nowiki>)

Keywords: Tumor-associated macrophages; Tumor progression; Cell cycle; Immunosuppression; CAR-M therapy

Dharaniya Sakthivel, Alexandra Brown-Suedel, Lisa Bouchier-Hayes,

Chapter Seven - The role of the nucleolus in regulating the cell cycle and the DNA damage response,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 203-241,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2023.01.001</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162323000019</nowiki>)

Keywords: Nucleolus; Cell cycle; DNA damage; Nucleophosmin; Cancer; Ribosomal protein; p53; MDM2; p14-ARF

Abdol-Hossein Rezaeian, Hiroyuki Inuzuka, Wenyi Wei,

Chapter Six - Insights into the aberrant CDK4/6 signaling pathway as a therapeutic target in tumorigenesis,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 179-201,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2022.11.009</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162322000980</nowiki>)

Keywords: Cell cycle; Cyclin D; CDK4/6; Cancer therapy; Drug resistance; Ubiquitination

Copyright,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Page iv,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/S1876-1623(23)00054-8</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162323000548</nowiki>)

D. Thirumal Kumar, Nishaat Shaikh, R. Bithia, V. Karthick, C. George Priya Doss, R. Magesh,

Chapter Three - Computational screening and structural analysis of Gly201Arg and Gly201Asp missense mutations in human cyclin-dependent kinase 4 protein,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 57-96,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2023.02.002</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162323000147</nowiki>)

Keywords: Cyclin-dependent kinase 4; SNPs; Pathogenicity; Stability; Amino acid conservation; Physico-chemical properties; Molecular dynamics

Chandrabose Selvaraj,

Chapter Ten - Therapeutic targets in cancer treatment: Cell cycle proteins,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 313-342,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2023.02.003</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162323000159</nowiki>)

Keywords: Cell-cycle; CDKs; Solid tumors; CDKs inhibitors; Flavopiridol; UCN-01

Seyede Nazanin Zarneshan, Sajad Fakhri, Gabrielle Bachtel, Anupam Bishayee,

Chapter One - Exploiting pivotal mechanisms behind the senescence-like cell cycle arrest in cancer,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 1-19,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2022.11.007</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162322000967</nowiki>)

Keywords: Cellular senescence; Cell cycle arrest; Apoptosis; Signaling pathway; Pharmacology; Cancer; Tumor

Anastas Gospodinov, Stefka Dzhokova, Maria Petrova, Iva Ugrinova,

Chapter Eight - Chromatin regulators in DNA replication and genome stability maintenance during S-phase,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 243-280,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2023.02.012</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162323000330</nowiki>)

Keywords: DNA replication; DNA replication stress; Genome stability; Histone post-translational modifications; Chromatin remodeling; Chromatin dynamics; Replication-transcription conflicts

Contributors,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages xi-xv,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/S1876-1623(23)00056-1</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162323000561</nowiki>)

N. Madhana Priya, Ambritha Balasundaram, N. Sidharth Kumar, S. Udhaya Kumar, D. Thirumal Kumar, R. Magesh, Hatem Zayed, C. George Priya Doss,

Chapter Four - Controlling cell proliferation by targeting cyclin-dependent kinase 6 using drug repurposing approach,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 97-124,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2023.01.003</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162323000123</nowiki>)

Keywords: CDK6; Breast cancer; Molecular docking; Molecular dynamics simulations; Candidate molecules

Nilmani, Maria D'costa, Anusha Bothe, Soumik Das, S. Udhaya Kumar, R. Gnanasambandan, C. George Priya Doss,

Chapter Five - CDK regulators—Cell cycle progression or apoptosis—Scenarios in normal cells and cancerous cells,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 125-177,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2022.11.008</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162322000979</nowiki>)

Keywords: CDKs; CKIs; Cell cycle; Pan-CDK inhibitors; Apoptosis; Ribosomal protein inhibiting CDKs; Therapeutics

Ashna Gupta, Gunjan Dagar, Ravi Chauhan, Hana Q. Sadida, Sara K. Almarzooqi, Sheema Hashem, Shahab Uddin, Muzafar A. Macha, Ammira S. Al-Shabeeb Akil, Tej K. Pandita, Ajaz A. Bhat, Mayank Singh,

Chapter Two - Cyclin-dependent kinases in cancer: Role, regulation, and therapeutic targeting,

Editor(s): Rossen Donev,

Advances in Protein Chemistry and Structural Biology,

Academic Press,

Volume 135,

2023,

Pages 21-55,

ISSN 1876-1623,

<nowiki>ISBN 9780443158223</nowiki>,

<nowiki>https://doi.org/10.1016/bs.apcsb.2023.02.001</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S1876162323000135</nowiki>)

Keywords: Apoptosis; Cancer; Cell proliferation; Cell division; Cyclins; Cyclin-dependent kinases</ref> In addition, the linker before the BCCP core in the holoenzyme could also be flexible, which would give further reach for the biotin N1′ atom.<ref>{{Cite web |title=Biotin Carboxyl Carrier Protein - an overview {{!}} ScienceDirect Topics |url=https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/biotin-carboxyl-carrier-protein |access-date=2023-04-26 |website=www.sciencedirect.com}}</ref>

The structures of biotin-accepting domains from ''E. coli'' BCCP-87 and the 1.3S subunit of ''P. shermanii'' TC were determined by both X-ray crystallography and nuclear magnetic resonance studies. (Athappilly and Hendrickson, 1995; Roberts ''et al''., 1999; Reddy ''et al''., 1998).<ref>Charles O. Rock, Suzanne Jackowski, John E. Cronan,

Chapter 2 - Lipid metabolism in prokaryotes,

Editor(s): Dennis E. Vance, Jean E. Vance,

New Comprehensive Biochemistry,

Elsevier,

Volume 31,

1996,

Pages 35-74,

ISSN 0167-7306,

<nowiki>ISBN 9780444823595</nowiki>,

<nowiki>https://doi.org/10.1016/S0167-7306(08)60509-8</nowiki>.

(<nowiki>https://www.sciencedirect.com/science/article/pii/S0167730608605098</nowiki>)</ref> These produced essentially the same structures that are structurally related to the lipoyl domains of 2-oxo acid dehydrogenase multienzyme complexes (Brocklehurst and Perham, 1993; Dardel ''et al''., 1993), which similarly undergo an analogous post-translational modification. These domains form a flattened β-barrel structure comprising two four-stranded β-sheets with the N- and C-terminal residues close together at one end of the structure. At the other end of the molecule, the biotinyl- or lipoyl-accepting lysine resides on a highly exposed, tight hairpin loop between β4 and β5 strands. The structure of the domain is stabilized by a core of hydrophobic residues, which are important structural determinants. Conserved glycine residues occupy β-turns linking the β-strands.<ref>Lennarz, William J., and M. Daniel Lane. ''Encyclopedia of Biological Chemistry''. Elsevier, 2013. </ref>
[[Category:Coenzymes]]
[[Category:Coenzymes]]
[[Category:Enzymes]]
[[Category:Enzymes]]

Revision as of 18:45, 26 April 2023

"BCCP" redirects here. For the cricket board, see Pakistan Cricket Board.
Biotin Carboxyl Carrier Protein

Biotin Carboxyl Carrier Protein (BCCP) refers to proteins containing a biotin attachment domain that carry biotin and carboxybiotin throughout the ATP-dependent carboxylation by biotin-dependent carboxylases. The biotin carboxyl carrier protein is an Acetyl CoA subunit that allows for Acetyl CoA to be catalyzed and converted to malonyl-CoA. More specifically, BCCP catalyzes the carboxylation of the carrier protein to form an intermediate. Then the carboxyl group is transferred by the transcacrboxylase to form the malonyl-CoA.[1] This conversion is an essential step in the biosynthesis of fatty acids. In the case of E. coli Acetyl-CoA carboxylase, the BCCP is a separate protein known as accB (P0ABD8). On the other hand, in Haloferax mediterranei Propionyl-CoA carboxylase, the BCCP pccA (I3R7G3) is fused with biotin carboxylase.

The biosynthesis of fatty acids in plants, such as triacylglycerol, is vital to the plant's overall health because it allows for accumulation of seed oil. The biosynthesis that is catalyzed by BCCP usually takes place in the chloroplast of plant cells. The biosynthesis performed by the BCCP protein allows for the transfer of CO2 within active sites of the cell.[2]

The biotin carboxyl carrier protein carries approximately 1 mol of biotin per 22,000 g of protein.[3]

There is not much research on BCCPs at the moment. However, a recent study[4]

on plant genomics found that Brassica BCCPs might play a key role in abiotic and biotic stress responses. Meaning that these proteins may be relaying messages to the rest of the plant body after it has been exposed to extreme conditions that disrupt the plant's homeostasis.

Structure

The first report of the BCCP structure was made by biochemists F. K. Athappilly and W. A. Hendrickson in 1995.[5] It can be thought of as a long β-hairpin structure, with four pairs of antiparallel β-strands that wrap around a central hydrophobic core. The biotinylation motif Met-Lys-Met is located at the tip of the β-hairpin structure. Rotations around the CαCβ bond of this Lys residue contribute to the swinging-arm model. The connection to the rest of the enzyme at the N-terminus of BCCP core is located at the opposite end of the structure from the biotin moiety. Rotations around this region contribute to the swinging-domain model, and the N1′ atom of biotin is ~ 40 Å from this pivot point. This gives a range of ~ 80 Å for the swinging-domain model, and the BC–CT active site distances observed so far are between 40 and 80 Å.[6] In addition, the linker before the BCCP core in the holoenzyme could also be flexible, which would give further reach for the biotin N1′ atom.[7]

The structures of biotin-accepting domains from E. coli BCCP-87 and the 1.3S subunit of P. shermanii TC were determined by both X-ray crystallography and nuclear magnetic resonance studies. (Athappilly and Hendrickson, 1995; Roberts et al., 1999; Reddy et al., 1998).[8] These produced essentially the same structures that are structurally related to the lipoyl domains of 2-oxo acid dehydrogenase multienzyme complexes (Brocklehurst and Perham, 1993; Dardel et al., 1993), which similarly undergo an analogous post-translational modification. These domains form a flattened β-barrel structure comprising two four-stranded β-sheets with the N- and C-terminal residues close together at one end of the structure. At the other end of the molecule, the biotinyl- or lipoyl-accepting lysine resides on a highly exposed, tight hairpin loop between β4 and β5 strands. The structure of the domain is stabilized by a core of hydrophobic residues, which are important structural determinants. Conserved glycine residues occupy β-turns linking the β-strands.[9]


Stub icon

This enzyme-related article is a stub. You can help Wikipedia by expanding it.

Stub icon

This protein-related article is a stub. You can help Wikipedia by expanding it.

  1. ^ "UniProt". www.uniprot.org. Retrieved 2023-04-26.
  2. ^ "InterPro". www.ebi.ac.uk. Retrieved 2023-04-26.
  3. ^ Fall, R. Ray; Nervi, A. M.; Alberts, Alfred W.; Vagelos, P. Roy (1971-07). "Acetyl CoA Carboxylase: Isolation and Characterization of Native Biotin Carboxyl Carrier Protein". Proceedings of the National Academy of Sciences. 68 (7): 1512–1515. doi:10.1073/pnas.68.7.1512. ISSN 0027-8424. PMC 389229. PMID 4934522. {{cite journal}}: Check date values in: |date= (help)CS1 maint: PMC format (link)
  4. ^ Megha, Swati; Wang, Zhengping; Kav, Nat N. V.; Rahman, Habibur (2022-10-17). "Genome-wide identification of biotin carboxyl carrier subunits of acetyl-CoA carboxylase in Brassica and their role in stress tolerance in oilseed Brassica napus". BMC Genomics. 23 (1): 707. doi:10.1186/s12864-022-08920-y. ISSN 1471-2164.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  5. ^ Athappilly, F. K.; Hendrickson, W. A. (1995-12-15). "Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing". Structure (London, England: 1993). 3 (12): 1407–1419. doi:10.1016/s0969-2126(01)00277-5. ISSN 0969-2126. PMID 8747466.
  6. ^ Chareeporn Akekawatchai, Sarawut Jitrapakdee, Chapter Twelve - Cellular signals integrate cell cycle and metabolic control in cancer, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 397-423, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2023.01.002. (https://www.sciencedirect.com/science/article/pii/S1876162323000020) Keywords: Cancer; Growth factors; Receptor tyrosine kinase; Cell cycle; Metabolism; Apoptosis Debarun Patra, Kumari Bhavya, Palla Ramprasad, Moyna Kalia, Durba Pal, Chapter Eleven - Anti-cancer drug molecules targeting cancer cell cycle and proliferation, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 343-395, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2022.11.011. (https://www.sciencedirect.com/science/article/pii/S1876162322001006) Keywords: Cancer cells; Cell cycle; Cell proliferation; Targeted therapy; Checkpoint inhibitors Mamta Panda, Elora Kalita, Abhishek Rao, Vijay Kumar Prajapati, Chapter Fourteen - Mechanism of cell cycle regulation and cell proliferation during human viral infection, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 497-525, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2022.11.013. (https://www.sciencedirect.com/science/article/pii/S187616232200102X) Keywords: Cell cycle; Viral regulation; Immune checkpoints; DNA viruses; RNA viruses; Host pathogen interaction Esra Albayrak, Fatih Kocabaş, Chapter Thirteen - Therapeutic targeting and HSC proliferation by small molecules and biologicals, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 425-496, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2022.11.012. (https://www.sciencedirect.com/science/article/pii/S1876162322001018) Keywords: Hematopoietic stem cells; Small molecule; Ex vivo expansion; HSC transplantation Leena Arora, Moyna Kalia, Durba Pal, Chapter Nine - Role of macrophages in cancer progression and targeted immunotherapies, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 281-311, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2022.11.010. (https://www.sciencedirect.com/science/article/pii/S1876162322000992) Keywords: Tumor-associated macrophages; Tumor progression; Cell cycle; Immunosuppression; CAR-M therapy Dharaniya Sakthivel, Alexandra Brown-Suedel, Lisa Bouchier-Hayes, Chapter Seven - The role of the nucleolus in regulating the cell cycle and the DNA damage response, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 203-241, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2023.01.001. (https://www.sciencedirect.com/science/article/pii/S1876162323000019) Keywords: Nucleolus; Cell cycle; DNA damage; Nucleophosmin; Cancer; Ribosomal protein; p53; MDM2; p14-ARF Abdol-Hossein Rezaeian, Hiroyuki Inuzuka, Wenyi Wei, Chapter Six - Insights into the aberrant CDK4/6 signaling pathway as a therapeutic target in tumorigenesis, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 179-201, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2022.11.009. (https://www.sciencedirect.com/science/article/pii/S1876162322000980) Keywords: Cell cycle; Cyclin D; CDK4/6; Cancer therapy; Drug resistance; Ubiquitination Copyright, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Page iv, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/S1876-1623(23)00054-8. (https://www.sciencedirect.com/science/article/pii/S1876162323000548) D. Thirumal Kumar, Nishaat Shaikh, R. Bithia, V. Karthick, C. George Priya Doss, R. Magesh, Chapter Three - Computational screening and structural analysis of Gly201Arg and Gly201Asp missense mutations in human cyclin-dependent kinase 4 protein, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 57-96, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2023.02.002. (https://www.sciencedirect.com/science/article/pii/S1876162323000147) Keywords: Cyclin-dependent kinase 4; SNPs; Pathogenicity; Stability; Amino acid conservation; Physico-chemical properties; Molecular dynamics Chandrabose Selvaraj, Chapter Ten - Therapeutic targets in cancer treatment: Cell cycle proteins, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 313-342, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2023.02.003. (https://www.sciencedirect.com/science/article/pii/S1876162323000159) Keywords: Cell-cycle; CDKs; Solid tumors; CDKs inhibitors; Flavopiridol; UCN-01 Seyede Nazanin Zarneshan, Sajad Fakhri, Gabrielle Bachtel, Anupam Bishayee, Chapter One - Exploiting pivotal mechanisms behind the senescence-like cell cycle arrest in cancer, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 1-19, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2022.11.007. (https://www.sciencedirect.com/science/article/pii/S1876162322000967) Keywords: Cellular senescence; Cell cycle arrest; Apoptosis; Signaling pathway; Pharmacology; Cancer; Tumor Anastas Gospodinov, Stefka Dzhokova, Maria Petrova, Iva Ugrinova, Chapter Eight - Chromatin regulators in DNA replication and genome stability maintenance during S-phase, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 243-280, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2023.02.012. (https://www.sciencedirect.com/science/article/pii/S1876162323000330) Keywords: DNA replication; DNA replication stress; Genome stability; Histone post-translational modifications; Chromatin remodeling; Chromatin dynamics; Replication-transcription conflicts Contributors, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages xi-xv, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/S1876-1623(23)00056-1. (https://www.sciencedirect.com/science/article/pii/S1876162323000561) N. Madhana Priya, Ambritha Balasundaram, N. Sidharth Kumar, S. Udhaya Kumar, D. Thirumal Kumar, R. Magesh, Hatem Zayed, C. George Priya Doss, Chapter Four - Controlling cell proliferation by targeting cyclin-dependent kinase 6 using drug repurposing approach, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 97-124, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2023.01.003. (https://www.sciencedirect.com/science/article/pii/S1876162323000123) Keywords: CDK6; Breast cancer; Molecular docking; Molecular dynamics simulations; Candidate molecules Nilmani, Maria D'costa, Anusha Bothe, Soumik Das, S. Udhaya Kumar, R. Gnanasambandan, C. George Priya Doss, Chapter Five - CDK regulators—Cell cycle progression or apoptosis—Scenarios in normal cells and cancerous cells, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 125-177, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2022.11.008. (https://www.sciencedirect.com/science/article/pii/S1876162322000979) Keywords: CDKs; CKIs; Cell cycle; Pan-CDK inhibitors; Apoptosis; Ribosomal protein inhibiting CDKs; Therapeutics Ashna Gupta, Gunjan Dagar, Ravi Chauhan, Hana Q. Sadida, Sara K. Almarzooqi, Sheema Hashem, Shahab Uddin, Muzafar A. Macha, Ammira S. Al-Shabeeb Akil, Tej K. Pandita, Ajaz A. Bhat, Mayank Singh, Chapter Two - Cyclin-dependent kinases in cancer: Role, regulation, and therapeutic targeting, Editor(s): Rossen Donev, Advances in Protein Chemistry and Structural Biology, Academic Press, Volume 135, 2023, Pages 21-55, ISSN 1876-1623, ISBN 9780443158223, https://doi.org/10.1016/bs.apcsb.2023.02.001. (https://www.sciencedirect.com/science/article/pii/S1876162323000135) Keywords: Apoptosis; Cancer; Cell proliferation; Cell division; Cyclins; Cyclin-dependent kinases
  7. ^ "Biotin Carboxyl Carrier Protein - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 2023-04-26.
  8. ^ Charles O. Rock, Suzanne Jackowski, John E. Cronan, Chapter 2 - Lipid metabolism in prokaryotes, Editor(s): Dennis E. Vance, Jean E. Vance, New Comprehensive Biochemistry, Elsevier, Volume 31, 1996, Pages 35-74, ISSN 0167-7306, ISBN 9780444823595, https://doi.org/10.1016/S0167-7306(08)60509-8. (https://www.sciencedirect.com/science/article/pii/S0167730608605098)
  9. ^ Lennarz, William J., and M. Daniel Lane. Encyclopedia of Biological Chemistry. Elsevier, 2013.
Retrieved from "https://en.wikipedia.org/w/index.php?title=Biotin_carboxyl_carrier_protein&oldid=1151864603"