EC Tree |
3. Hydrolases |
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
3.5.4 In cyclic amidines |
ID: | 3.5.4.10 |
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Description: | IMP cyclohydrolase. |
Alternative Name: |
Inosinicase. IMP synthetase. |
Cath: | 1.10.287.440; 3.60.20.20; 3.40.140.20; 3.40.50.1380; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 3.5.4.10 |
BRENDA Enzyme Link: | BRENDA 3.5.4.10 |
KEGG Enzyme Link: | KEGG3.5.4.10 |
BioCyc Enzyme Link: | BioCyc 3.5.4.10 |
ExPASy Enzyme Link: | ExPASy3.5.4.10 |
EC2PDB Enzyme Link: | EC2PDB 3.5.4.10 |
ExplorEnz Enzyme Link: | ExplorEnz 3.5.4.10 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.5.4.10 |
IntEnz Enzyme Link: | IntEnz 3.5.4.10 |
MEDLINE Enzyme Link: | MEDLINE 3.5.4.10 |
RHEA:18445 | H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide |
RULE(radius=1) | [*:1]=[c;H0;+0:2]1:[*:3]:[*:4]:[n;H0;+0:5]:[cH;+0:6]:[nH;+0:7]:1.[OH2;+0:8]>>[*:1]=[C;H0;+0:2](-[NH2;+0:7])-[*:3]:[*:4]-[NH;+0:5]-[CH;+0:6]=[O;H0;+0:8] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Structural analyses of a purine biosynthetic enzyme from Mycobacterium tuberculosis reveal a novel bound nucleotide. | Le Nours J, Bulloch EM, Zhang Z, Greenwood DR, Middleditch MJ, Dickson JM, Baker EN | 2011 Nov 25 | 21956117 |
Catalytic mechanism of the cyclohydrolase activity of human aminoimidazole carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase. | Vergis JM, Beardsley GP | 2004 Feb 10 | 14756554 |
Biosynthesis of the purines. XVIII. 5-Amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase and inosinicase. | FLAKS JG, ERWIN MJ, BUCHANAN JM | 1957 Dec | 13502325 |