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'''BpsA''' (N(4)-bis(aminopropyl)spermidine synthase) is a single-module non-ribosomal peptide synthase (NRPS) (also see [[Nonribosomal peptide|non-ribosomal peptide (NPR)]]) located in the cytoplasm<ref name=":2" /> responsible for the process of creating branched-chain polyamines,<ref name=":2">{{Cite web |title=UniProt |url=https://www.uniprot.org/uniprotkb/Q58669/entry#family_and_domains |access-date=2022-09-30 |website=www.uniprot.org}}</ref> and producing spermidine and spermine.<ref name=":1">{{Cite journal | |
'''BpsA''' (N(4)-bis(aminopropyl)spermidine synthase) is a single-module non-ribosomal peptide synthase (NRPS) (also see [[Nonribosomal peptide|non-ribosomal peptide (NPR)]]) located in the cytoplasm<ref name=":2" /> responsible for the process of creating branched-chain polyamines,<ref name=":2">{{Cite web |title=UniProt |url=https://www.uniprot.org/uniprotkb/Q58669/entry#family_and_domains |access-date=2022-09-30 |website=www.uniprot.org}}</ref> and producing spermidine and spermine.<ref name=":1">{{Cite journal |last1=Okada |first1=Kazuma |last2=Hidese |first2=Ryota |last3=Fukuda |first3=Wakao |last4=Niitsu |first4=Masaru |last5=Takao |first5=Koichi |last6=Horai |first6=Yuhei |last7=Umezawa |first7=Naoki |last8=Higuchi |first8=Tsunehiko |last9=Oshima |first9=Tairo |last10=Yoshikawa |first10=Yuko |last11=Imanaka |first11=Tadayuki |last12=Fujiwara |first12=Shinsuke |date=2014-05-15 |title=Identification of a Novel Aminopropyltransferase Involved in the Synthesis of Branched-Chain Polyamines in Hyperthermophiles |journal=Journal of Bacteriology |language=en |volume=196 |issue=10 |pages=1866–1876 |doi=10.1128/JB.01515-14 |issn=0021-9193 |pmc=4010994 |pmid=24610711}}</ref> It has a singular ligand in it's structure involved with Fe3+ and PLIP interactions.<ref>{{Cite web |title=6AF45151B678865CD36DEBB6EF9E7335 {{!}} SWISS-MODEL Repository |url=https://swissmodel.expasy.org/repository/md5/6af45151b678865cd36debb6ef9e7335?template=2qm3 |access-date=2022-09-30 |website=swissmodel.expasy.org}}</ref> As seen by it's EC number, it is a transferase (2) that transfers an alkyl or aryl group other than methyl groups (5) (2.5.1).{{cn|date=October 2022}} BpsA was first discovered in the archaea ''[[Methanocaldococcus jannaschii|Methanococcus jannaschii]]''<ref>{{Cite journal |last1=Bult |first1=Carol J. |last2=White |first2=Owen |last3=Olsen |first3=Gary J. |last4=Zhou |first4=Lixin |last5=Fleischmann |first5=Robert D. |last6=Sutton |first6=Granger G. |last7=Blake |first7=Judith A. |last8=FitzGerald |first8=Lisa M. |last9=Clayton |first9=Rebecca A. |last10=Gocayne |first10=Jeannine D. |last11=Kerlavage |first11=Anthony R. |last12=Dougherty |first12=Brian A. |last13=Tomb |first13=Jean-Francois |last14=Adams |first14=Mark D. |last15=Reich |first15=Claudia I. |date=1996-08-23 |title=Complete Genome Sequence of the Methanogenic Archaeon, Methanococcus jannaschii |url=https://www.science.org/doi/10.1126/science.273.5278.1058 |journal=Science |language=en |volume=273 |issue=5278 |pages=1058–1073 |doi=10.1126/science.273.5278.1058 |pmid=8688087 |bibcode=1996Sci...273.1058B |s2cid=41481616 |issn=0036-8075}}</ref> and thermophile ''[[Thermococcus kodakarensis]]'' <ref name=":1" /> and since then has been used in a variety of applications such as being used as a reporter, researching phosphopantetheinyl transferase (PPTase), and for NRPS domain recombination experiments it can be used as a model.<ref name=":0">{{Cite journal |last1=Brown |first1=Alistair S. |last2=Robins |first2=Katherine J. |last3=Ackerley |first3=David F. |date=March 2017 |title=A sensitive single-enzyme assay system using the non-ribosomal peptide synthetase BpsA for measurement of L-glutamine in biological samples |journal=Scientific Reports |language=en |volume=7 |issue=1 |pages=41745 |doi=10.1038/srep41745 |issn=2045-2322 |pmc=5282505 |pmid=28139746|bibcode=2017NatSR...741745B }}</ref> Both (hyper)thermophilic bacteria and euryarchaeotal archaea seem to conserve BpsA and orthologs as branches chains polyamines are crucial for survival.<ref>{{Citation |last1=Hidese |first1=Ryota |title=Identification of Branched-Chain Polyamines in Hyperthermophiles |date=2018 |url=https://doi.org/10.1007/978-1-4939-7398-9_8 |work=Polyamines: Methods and Protocols |pages=81–94 |editor-last=Alcázar |editor-first=Rubén |place=New York, NY |publisher=Springer |language=en |doi=10.1007/978-1-4939-7398-9_8 |isbn=978-1-4939-7398-9 |access-date=2022-09-30 |last2=Fukuda |first2=Wakao |last3=Niitsu |first3=Masaru |last4=Fujiwara |first4=Shinsuke |volume=1694 |pmid=29080158 |editor2-last=Tiburcio |editor2-first=Antonio F.}}</ref> There is also a second type of BpsA also known as Blue-pigment indigoidine synthetase that produces the pigment indigoidine and is found in organisms like ''[[Erwinia chrysanthemi]].''<ref>{{Cite journal |last1=Reverchon |first1=Sylvie |last2=Rouanet |first2=Carine |last3=Expert |first3=Dominique |last4=Nasser |first4=William |date=February 2002 |title=Characterization of Indigoidine Biosynthetic Genes in Erwinia chrysanthemi and Role of This Blue Pigment in Pathogenicity |journal=Journal of Bacteriology |language=en |volume=184 |issue=3 |pages=654–665 |doi=10.1128/JB.184.3.654-665.2002 |issn=0021-9193 |pmc=139515 |pmid=11790734}}</ref> However, not much seems to be known about this variant except that it is a synthase, and it does not yet appear to be classified under an EC number. |
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==Thermophiles== |
==Thermophiles== |
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In thermophiles, BpsA converts ''N''4-aminopropylspermidine to ''N''4-bis(aminopropyl)spermidine.<ref name=":1" /> In this pathway, aminopropyltransferase and ureohydrolase turn ''N''1-aminopropylagmatine to agmantine and synthesize spermidine and spermine.<ref name=":1" /> Spermine and spermadine are utilized in a variety of pathways including macromolecule production, apoptosis and proliferation equilibrium, and the induction of differentiation in cells.<ref name=":5">{{Cite journal | |
In thermophiles, BpsA converts ''N''4-aminopropylspermidine to ''N''4-bis(aminopropyl)spermidine.<ref name=":1" /> In this pathway, aminopropyltransferase and ureohydrolase turn ''N''1-aminopropylagmatine to agmantine and synthesize spermidine and spermine.<ref name=":1" /> Spermine and spermadine are utilized in a variety of pathways including macromolecule production, apoptosis and proliferation equilibrium, and the induction of differentiation in cells.<ref name=":5">{{Cite journal |last1=Terui |first1=Yusuke |last2=Ohnuma |first2=Mio |last3=Hiraga |first3=Kaori |last4=Kawashima |first4=Etsuko |last5=Oshima |first5=Tairo |date=2005-06-01 |title=Stabilization of nucleic acids by unusual polyamines produced by an extreme thermophile, Thermus thermophilus |url=https://portlandpress.com/biochemj/article/388/2/427/93250/Stabilization-of-nucleic-acids-by-unusual |journal=Biochemical Journal |language=en |volume=388 |issue=2 |pages=427–433 |doi=10.1042/BJ20041778 |issn=0264-6021 |pmc=1138949 |pmid=15673283}}</ref> Long Linear polyamines (such as ones found in ''TK-''BpsA made of up spermine and spermidine) help stabilize DNA.<ref name=":5" /> Denaturation could possible occur at high temperatures, making the stabilization crucial for organisms that thrive here. If an organism cannot stabilize it's DNA, it cannot survive. ''TK-''BpsA is a BpsA found in the archaeon ''Thermococcus kodakarensis'' and is used to study this pathway more in depth.<ref name=":3">{{Cite journal |last1=Hidese |first1=Ryota |last2=Tse |first2=Ka |last3=Kimura |first3=Seigo |last4=Mizohata |first4=Eiichi |last5=Fujita |first5=Junso |last6=Horai |first6=Yuhei |last7=Umezawa |first7=Naoki |last8=Higuchi |first8=Tsunehiko |last9=Niitsu |first9=Masaru |last10=Oshima |first10=Tairo |last11=Imanaka |first11=Tadayuki |last12=Inoue |first12=Tsuyoshi |last13=Fujiwara |first13=Shinsuke |date=2017 |title=Active site geometry of a novel aminopropyltransferase for biosynthesis of hyperthermophile-specific branched-chain polyamine |url=https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.14262 |journal=The FEBS Journal |volume=284 |issue=21 |pages=3684–3701|doi=10.1111/febs.14262 |pmid=28881427 |s2cid=4027428 }}</ref> It is also a ternary complex.<ref name=":4" /> There are a few active sites that include polyamine spermidine/spermine synthases, and loop-closures occur upon the binding of spermidine, and a catalytic center made of a Gly-Asp-Asp-Asp motif which contains reactive secondary amino group of the substrate polyamine and a sulfur atom of the product 5ʹ-methylthioadenosine with Asp 159.<ref name=":3" /> The enzyme proves itself to be important to thermophiles as it supports growth under high-temperature conditions.<ref name=":2" /> In this system, the C-Terminal is a flexible region of branched-chain polyamine synthase facilitates substrate specificity and catalysis.<ref name=":4">{{Cite journal |last1=Hidese |first1=Ryota |last2=Toyoda |first2=Masataka |last3=Yoshino |first3=Ken‐ichi |last4=Fukuda |first4=Wakao |last5=Wihardja |first5=Gita Adhirani |last6=Kimura |first6=Seigo |last7=Fujita |first7=Junso |last8=Niitsu |first8=Masaru |last9=Oshima |first9=Tairo |last10=Imanaka |first10=Tadayuki |last11=Mizohata |first11=Eiichi |last12=Fujiwara |first12=Shinsuke |date=October 2019 |title=The C‐terminal flexible region of branched‐chain polyamine synthase facilitates substrate specificity and catalysis |url=https://onlinelibrary.wiley.com/doi/10.1111/febs.14949 |journal=The FEBS Journal |language=en |volume=286 |issue=19 |pages=3926–3940 |doi=10.1111/febs.14949 |pmid=31162806 |s2cid=174808703 |issn=1742-464X}}</ref> This C-terminal region recognizes acceptor proteins for the enzyme and gain their flexibility from aspartate/glutamate residues.<ref name=":4" /> The flexibility itself is promoted by a ping-pong Bi-Bi mechanism that occurs when temperatures are high.<ref name=":4" /> |
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==References== |
==References== |
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Revision as of 04:36, 23 October 2022
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BpsA (N(4)-bis(aminopropyl)spermidine synthase) is a single-module non-ribosomal peptide synthase (NRPS) (also see non-ribosomal peptide (NPR)) located in the cytoplasm[1] responsible for the process of creating branched-chain polyamines,[1] and producing spermidine and spermine.[2] It has a singular ligand in it's structure involved with Fe3+ and PLIP interactions.[3] As seen by it's EC number, it is a transferase (2) that transfers an alkyl or aryl group other than methyl groups (5) (2.5.1).[citation needed] BpsA was first discovered in the archaea Methanococcus jannaschii[4] and thermophile Thermococcus kodakarensis [2] and since then has been used in a variety of applications such as being used as a reporter, researching phosphopantetheinyl transferase (PPTase), and for NRPS domain recombination experiments it can be used as a model.[5] Both (hyper)thermophilic bacteria and euryarchaeotal archaea seem to conserve BpsA and orthologs as branches chains polyamines are crucial for survival.[6] There is also a second type of BpsA also known as Blue-pigment indigoidine synthetase that produces the pigment indigoidine and is found in organisms like Erwinia chrysanthemi.[7] However, not much seems to be known about this variant except that it is a synthase, and it does not yet appear to be classified under an EC number.
| Identifiers | |
|---|---|
| EC Number | 2.5.1.128 |
| Alt. Name | Branched-chain polyamine synthase A |
| Pathway(s) | Amine and Polyamine Biosynthesis |
| Molecular Function | Transferase |
| Gene Locus | MJ1273 |
Thermophiles
In thermophiles, BpsA converts N4-aminopropylspermidine to N4-bis(aminopropyl)spermidine.[2] In this pathway, aminopropyltransferase and ureohydrolase turn N1-aminopropylagmatine to agmantine and synthesize spermidine and spermine.[2] Spermine and spermadine are utilized in a variety of pathways including macromolecule production, apoptosis and proliferation equilibrium, and the induction of differentiation in cells.[8] Long Linear polyamines (such as ones found in TK-BpsA made of up spermine and spermidine) help stabilize DNA.[8] Denaturation could possible occur at high temperatures, making the stabilization crucial for organisms that thrive here. If an organism cannot stabilize it's DNA, it cannot survive. TK-BpsA is a BpsA found in the archaeon Thermococcus kodakarensis and is used to study this pathway more in depth.[9] It is also a ternary complex.[10] There are a few active sites that include polyamine spermidine/spermine synthases, and loop-closures occur upon the binding of spermidine, and a catalytic center made of a Gly-Asp-Asp-Asp motif which contains reactive secondary amino group of the substrate polyamine and a sulfur atom of the product 5ʹ-methylthioadenosine with Asp 159.[9] The enzyme proves itself to be important to thermophiles as it supports growth under high-temperature conditions.[1] In this system, the C-Terminal is a flexible region of branched-chain polyamine synthase facilitates substrate specificity and catalysis.[10] This C-terminal region recognizes acceptor proteins for the enzyme and gain their flexibility from aspartate/glutamate residues.[10] The flexibility itself is promoted by a ping-pong Bi-Bi mechanism that occurs when temperatures are high.[10]
References
- ^ a b c d "UniProt". www.uniprot.org. Retrieved 2022-09-30.
- ^ a b c d Okada, Kazuma; Hidese, Ryota; Fukuda, Wakao; Niitsu, Masaru; Takao, Koichi; Horai, Yuhei; Umezawa, Naoki; Higuchi, Tsunehiko; Oshima, Tairo; Yoshikawa, Yuko; Imanaka, Tadayuki; Fujiwara, Shinsuke (2014-05-15). "Identification of a Novel Aminopropyltransferase Involved in the Synthesis of Branched-Chain Polyamines in Hyperthermophiles". Journal of Bacteriology. 196 (10): 1866–1876. doi:10.1128/JB.01515-14. ISSN 0021-9193. PMC 4010994. PMID 24610711.
- ^ "6AF45151B678865CD36DEBB6EF9E7335 | SWISS-MODEL Repository". swissmodel.expasy.org. Retrieved 2022-09-30.
- ^ Bult, Carol J.; White, Owen; Olsen, Gary J.; Zhou, Lixin; Fleischmann, Robert D.; Sutton, Granger G.; Blake, Judith A.; FitzGerald, Lisa M.; Clayton, Rebecca A.; Gocayne, Jeannine D.; Kerlavage, Anthony R.; Dougherty, Brian A.; Tomb, Jean-Francois; Adams, Mark D.; Reich, Claudia I. (1996-08-23). "Complete Genome Sequence of the Methanogenic Archaeon, Methanococcus jannaschii". Science. 273 (5278): 1058–1073. Bibcode:1996Sci...273.1058B. doi:10.1126/science.273.5278.1058. ISSN 0036-8075. PMID 8688087. S2CID 41481616.
- ^ Brown, Alistair S.; Robins, Katherine J.; Ackerley, David F. (March 2017). "A sensitive single-enzyme assay system using the non-ribosomal peptide synthetase BpsA for measurement of L-glutamine in biological samples". Scientific Reports. 7 (1): 41745. Bibcode:2017NatSR...741745B. doi:10.1038/srep41745. ISSN 2045-2322. PMC 5282505. PMID 28139746.
- ^ Hidese, Ryota; Fukuda, Wakao; Niitsu, Masaru; Fujiwara, Shinsuke (2018), Alcázar, Rubén; Tiburcio, Antonio F. (eds.), "Identification of Branched-Chain Polyamines in Hyperthermophiles", Polyamines: Methods and Protocols, vol. 1694, New York, NY: Springer, pp. 81–94, doi:10.1007/978-1-4939-7398-9_8, ISBN 978-1-4939-7398-9, PMID 29080158, retrieved 2022-09-30
- ^ Reverchon, Sylvie; Rouanet, Carine; Expert, Dominique; Nasser, William (February 2002). "Characterization of Indigoidine Biosynthetic Genes in Erwinia chrysanthemi and Role of This Blue Pigment in Pathogenicity". Journal of Bacteriology. 184 (3): 654–665. doi:10.1128/JB.184.3.654-665.2002. ISSN 0021-9193. PMC 139515. PMID 11790734.
- ^ a b Terui, Yusuke; Ohnuma, Mio; Hiraga, Kaori; Kawashima, Etsuko; Oshima, Tairo (2005-06-01). "Stabilization of nucleic acids by unusual polyamines produced by an extreme thermophile, Thermus thermophilus". Biochemical Journal. 388 (2): 427–433. doi:10.1042/BJ20041778. ISSN 0264-6021. PMC 1138949. PMID 15673283.
- ^ a b Hidese, Ryota; Tse, Ka; Kimura, Seigo; Mizohata, Eiichi; Fujita, Junso; Horai, Yuhei; Umezawa, Naoki; Higuchi, Tsunehiko; Niitsu, Masaru; Oshima, Tairo; Imanaka, Tadayuki; Inoue, Tsuyoshi; Fujiwara, Shinsuke (2017). "Active site geometry of a novel aminopropyltransferase for biosynthesis of hyperthermophile-specific branched-chain polyamine". The FEBS Journal. 284 (21): 3684–3701. doi:10.1111/febs.14262. PMID 28881427. S2CID 4027428.
- ^ a b c d Hidese, Ryota; Toyoda, Masataka; Yoshino, Ken‐ichi; Fukuda, Wakao; Wihardja, Gita Adhirani; Kimura, Seigo; Fujita, Junso; Niitsu, Masaru; Oshima, Tairo; Imanaka, Tadayuki; Mizohata, Eiichi; Fujiwara, Shinsuke (October 2019). "The C‐terminal flexible region of branched‐chain polyamine synthase facilitates substrate specificity and catalysis". The FEBS Journal. 286 (19): 3926–3940. doi:10.1111/febs.14949. ISSN 1742-464X. PMID 31162806. S2CID 174808703.