ID: | 4.3.3.1 |
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Description: | 3-ketovalidoxylamine C-N-lyase. |
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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 4.3.3.1 |
BRENDA Enzyme Link: | BRENDA 4.3.3.1 |
KEGG Enzyme Link: | KEGG4.3.3.1 |
BioCyc Enzyme Link: | BioCyc 4.3.3.1 |
ExPASy Enzyme Link: | ExPASy4.3.3.1 |
EC2PDB Enzyme Link: | EC2PDB 4.3.3.1 |
ExplorEnz Enzyme Link: | ExplorEnz 4.3.3.1 |
PRIAM enzyme-specific profiles Link: | PRIAM 4.3.3.1 |
IntEnz Enzyme Link: | IntEnz 4.3.3.1 |
MEDLINE Enzyme Link: | MEDLINE 4.3.3.1 |
RHEA:22768 | 4-nitrophenyl-3-ketovalidamine = 4-nitroaniline + 5D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one |
RULE(radius=1) | [*:1]-[CH;+0:2](-[NH;+0:3]-[*:4])-[CH;+0:5](-[*:6])-[*:7]>>[*:1]-[CH;+0:2]=[C;H0;+0:5](-[*:6])-[*:7].[*:4]-[NH2;+0:3] |
Reaction | ![]() |
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Core-to-Core |
Title | Authors | Date | PubMed ID |
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Microbial degradation of validamycin A by Flavobacterium saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A. | Asano N, Takeuchi M, Ninomiya K, Kameda Y, Matsui K | 1984 Aug | 6548220 |
Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum. | Takeuchi M, Asano N, Kameda Y, Matsui K | 1985 Dec | 4093450 |