Inosine monophosphate synthase: Difference between revisions

ATIC
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1P4R, 1PKX, 1PL0
Identifiers
Aliases	ATIC, AICAR, AICARFT, HEL-S-70p, IMPCHASE, PURH, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
External IDs	OMIM: 601731; MGI: 1351352; HomoloGene: 2983; GeneCards: ATIC; OMA:ATIC - orthologs
Gene location (Human)
Chr.	Chromosome 2 (human)
End	215,349,773 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	71,618,790 bp
RNA expression pattern
	Top expressed in
	mucosa of transverse colon; ; stromal cell of endometrium; ; rectum; ; anterior pituitary; ; ventricular zone; ; right adrenal cortex; ; body of pancreas; ; gonad; ; ganglionic eminence; ; left adrenal cortex;
	Top expressed in
	hand; ; epiblast; ; condyle; ; mandibular prominence; ; maxillary prominence; ; transitional epithelium of urinary bladder; ; abdominal wall; ; mesenteric lymph nodes; ; primitive streak; ; foot;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; protein homodimerization activity; IMP cyclohydrolase activity; catalytic activity; phosphoribosylaminoimidazolecarboxamide formyltransferase activity; hydrolase activity; cadherin binding;
Cellular component	cytosol; membrane; mitochondrion; extracellular exosome; plasma membrane;
Biological process	purine nucleotide biosynthetic process; dihydrofolate metabolic process; 'de novo' IMP biosynthetic process; brainstem development; ribonucleotide metabolic process; cerebellum development; nucleoside metabolic process; tetrahydrofolate biosynthetic process; animal organ regeneration; response to inorganic substance; cerebral cortex development; purine ribonucleoside monophosphate biosynthetic process; metabolism; nucleobase-containing compound metabolic process; cellular response to interleukin-7;
	Sources:Amigo / QuickGO
Orthologs
	471
	108147
	ENSG00000138363
	ENSMUSG00000026192
	P31939
	Q9CWJ9
	NM_004044
	NM_026195
	NP_004035
	NP_080471
	Wikidata
View/Edit Human	View/Edit Mouse

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Revision as of 00:47, 22 December 2007

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5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase, also known as ATIC and Inosine monophosphate synthase, is a human gene.^[5] Template:PBB Summary ATIC encodes an enzyme which generates inosine monophosphate from aminoimidazole carboxamide ribonucleotide.

It has two functions:

EC 2.1.2.3 - 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
EC 3.5.4.10 - IMP cyclohydrolase

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000138363 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026192 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: ATIC 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase".

External links

Inosine+monophosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This biochemistry article is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000138363 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000026192 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: ATIC 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase".

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@@ Line 58: / Line 58: @@
 * {{EC number|2.1.2.3}} - 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
 * {{EC number|3.5.4.10}} - IMP cyclohydrolase
+==References==
+{{reflist}}
+==Further reading==
+{{refbegin | 2}}
+{{PBB_Further_reading
+| citations =
+*{{cite journal  | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi=  }}
+*{{cite journal  | author=Rayl EA, Moroson BA, Beardsley GP |title=The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping. |journal=J. Biol. Chem. |volume=271 |issue= 4 |pages= 2225-33 |year= 1996 |pmid= 8567683 |doi=  }}
+*{{cite journal  | author=Yamauchi M, Seki N, Mita K, ''et al.'' |title=Isolation of human purH gene expressed in the rodent transformant cells by subtractive enrichment of 3'-untranslated region of human transcript. |journal=DNA Res. |volume=2 |issue= 6 |pages= 269-75 |year= 1996 |pmid= 8867801 |doi=  }}
+*{{cite journal  | author=Sugita T, Aya H, Ueno M, ''et al.'' |title=Characterization of molecularly cloned human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase. |journal=J. Biochem. |volume=122 |issue= 2 |pages= 309-13 |year= 1997 |pmid= 9378707 |doi=  }}
+*{{cite journal  | author=Beardsley GP, Rayl EA, Gunn K, ''et al.'' |title=Structure and functional relationships in human pur H. |journal=Adv. Exp. Med. Biol. |volume=431 |issue=  |pages= 221-6 |year= 1998 |pmid= 9598063 |doi=  }}
+*{{cite journal  | author=Vergis JM, Bulock KG, Fleming KG, Beardsley GP |title=Human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase. A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity. |journal=J. Biol. Chem. |volume=276 |issue= 11 |pages= 7727-33 |year= 2001 |pmid= 11096114 |doi= 10.1074/jbc.M009940200 }}
+*{{cite journal  | author=Bulock KG, Beardsley GP, Anderson KS |title=The kinetic mechanism of the human bifunctional enzyme ATIC (5-amino-4-imidazolecarboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase). A surprising lack of substrate channeling. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22168-74 |year= 2002 |pmid= 11948179 |doi= 10.1074/jbc.M111964200 }}
+*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
+*{{cite journal  | author=Cheong CG, Wolan DW, Greasley SE, ''et al.'' |title=Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates. |journal=J. Biol. Chem. |volume=279 |issue= 17 |pages= 18034-45 |year= 2004 |pmid= 14966129 |doi= 10.1074/jbc.M313691200 }}
+*{{cite journal  | author=Marie S, Heron B, Bitoun P, ''et al.'' |title=AICA-ribosiduria: a novel, neurologically devastating inborn error of purine biosynthesis caused by mutation of ATIC. |journal=Am. J. Hum. Genet. |volume=74 |issue= 6 |pages= 1276-81 |year= 2004 |pmid= 15114530 |doi= 10.1086/421475 }}
+*{{cite journal  | author=Dervieux T, Furst D, Lein DO, ''et al.'' |title=Polyglutamation of methotrexate with common polymorphisms in reduced folate carrier, aminoimidazole carboxamide ribonucleotide transformylase, and thymidylate synthase are associated with methotrexate effects in rheumatoid arthritis. |journal=Arthritis Rheum. |volume=50 |issue= 9 |pages= 2766-74 |year= 2004 |pmid= 15457444 |doi= 10.1002/art.20460 }}
+*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
+*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
+}}
+{{refend}}
 ==External links==

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase
3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase
3.5.5: Nitriles/ Aminohydrolases	Nitrilase
3.5.99: Other	Riboflavinase Thiaminase II