Due to improvement work scheduled on this server, some services may not be fully operational on Tuesday December 12 daytime (CEST).
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https

ENZYME entry: EC 4.1.1.77

Accepted Name
2-oxo-3-hexenedioate decarboxylase.
Alternative Name(s)
4-oxalocrotonate carboxy-lyase.
4-oxalocrotonate decarboxylase.
Reaction catalysed
(3E)-2-oxohex-3-enedioate <=> 2-oxopent-4-enoate + CO(2)
Comment(s)
  • Involved in the meta-cleavage pathway for the degradation of phenols, modified phenols and catechols.
  • The enzyme has been reported to accept multiple tautomeric forms.
  • However, careful analysis of the stability of the different tautomers, as well as characterization of the enzyme that produces its substrate, EC 5.3.2.6, showed that the actual substrate for the enzyme is (3E)-2-oxohex-3-enedioate.
Cross-references
BRENDA4.1.1.77
EC2PDB4.1.1.77
ExplorEnz4.1.1.77
PRIAM enzyme-specific profiles4.1.1.77
KEGG Ligand Database for Enzyme Nomenclature4.1.1.77
IUBMB Enzyme Nomenclature4.1.1.77
IntEnz4.1.1.77
MEDLINEFind literature relating to 4.1.1.77
MetaCyc4.1.1.77
UniProtKB/Swiss-Prot
Q9KWS3, AMNE_PSESP;  P49156, DMPH_PSEUF;  P49155, XYLI_PSEPU;  

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-