EC number:4.1.1.7

Enzyme

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EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.1 Carboxy-lyases
ID:4.1.1.7
Description:Benzoylformate decarboxylase.
Alternative Name: Benzoylformate carboxy-lyase.
Prosite: PDOC00166;
PDB:
PDBScop
Cath: 3.40.50.970; 3.40.50.1220;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.1.7
BRENDA Enzyme Link: BRENDA 4.1.1.7
KEGG Enzyme Link: KEGG4.1.1.7
BioCyc Enzyme Link: BioCyc 4.1.1.7
ExPASy Enzyme Link: ExPASy4.1.1.7
EC2PDB Enzyme Link: EC2PDB 4.1.1.7
ExplorEnz Enzyme Link: ExplorEnz 4.1.1.7
PRIAM enzyme-specific profiles Link: PRIAM 4.1.1.7
IntEnz Enzyme Link: IntEnz 4.1.1.7
MEDLINE Enzyme Link: MEDLINE 4.1.1.7

EC number:4.1.1.7

MSA:

4.1.1.7;
Phylogenetic Tree:

4.1.1.7;
Uniprot:
M-CSA:
RHEA:23368 H(+) + phenylglyoxylate = benzaldehyde + CO2
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[C;H0;+0:4](=[*:5])-[*:6].[H+;H0:7]>>[*:1]=[C;H0;+0:2]=[O;H0;+0:3].[*:5]=[CH;+0:4]-[*:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes.Hasson MS, Muscate A, McLeish MJ, Polovnikova LS, Gerlt JA, Kenyon GL, Petsko GA, Ringe D1998 Jul 149665697
Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analogues.Weiss PM, Garcia GA, Kenyon GL, Cleland WW, Cook PF1988 Mar 223378056