ID: | 4.1.99.19 |
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Description: | 2-iminoacetate synthase. |
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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 4.1.99.19 |
BRENDA Enzyme Link: | BRENDA 4.1.99.19 |
KEGG Enzyme Link: | KEGG4.1.99.19 |
BioCyc Enzyme Link: | BioCyc 4.1.99.19 |
ExPASy Enzyme Link: | ExPASy4.1.99.19 |
EC2PDB Enzyme Link: | EC2PDB 4.1.99.19 |
ExplorEnz Enzyme Link: | ExplorEnz 4.1.99.19 |
PRIAM enzyme-specific profiles Link: | PRIAM 4.1.99.19 |
IntEnz Enzyme Link: | IntEnz 4.1.99.19 |
MEDLINE Enzyme Link: | MEDLINE 4.1.99.19 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:26361 | L-tyrosine + NADPH + S-adenosyl-L-methionine = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + NADP(+) |
RULE(radius=1) | [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[*:5].[*:6]-[N;H0;+0:7]1-[CH;+0:8]=[C;H0;+0:9](-[*:10])-[CH2;+0:11]-[CH;+0:12]=[CH;+0:13]-1.[*:14]-[S+;H0:15](-[*:16])-[CH2;+0:17]-[*:18]>>[*:18]-[CH3;+0:17].[*:5]-[CH3;+0:4].[*:1]-[CH;+0:2]=[NH;+0:3].[*:14]-[S;H0;+0:15]-[*:16].[*:6]-[n+;H0:7]1:[cH;+0:8]:[c;H0;+0:9](-[*:10]):[cH;+0:11]:[cH;+0:12]:[cH;+0:13]:1 |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
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Catalytic activity of the anaerobic tyrosine lyase required for thiamine biosynthesis in Escherichia coli. | Challand MR, Martins FT, Roach PL | 2010 Feb 19 | 19923213 |
Thiamine biosynthesis in Escherichia coli: identification of the intermediate and by-product derived from tyrosine. | Kriek M, Martins F, Challand MR, Croft A, Roach PL | 2007 | 17969213 |
Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro. | Kriek M, Martins F, Leonardi R, Fairhurst SA, Lowe DJ, Roach PL | 2007 Jun 15 | 17403671 |
Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex. | Leonardi R, Fairhurst SA, Kriek M, Lowe DJ, Roach PL | 2003 Mar 27 | 12650933 |