From Wikipedia, the free encyclopedia
dimethylmaleate hydratase
Identifiers
EC no. 4.2.1.85
CAS no. 93229-56-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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NCBI proteins

The enzyme dimethylmaleate hydratase ( EC 4.2.1.85) catalyzes the chemical reaction

(2R,3S)-2,3-dimethylmalate dimethylmaleate + H2O

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (2R,3S)-2,3-dimethylmalate hydro-lyase (dimethylmaleate-forming). This enzyme is also called (2R,3S)-2,3-dimethylmalate hydro-lyase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, iron.

References

  • Kollmann-Koch A, Eggerer H (1984). "Nicotinic acid metabolism. Dimethylmaleate hydratase". Hoppe-Seyler's Z. Physiol. Chem. 365 (8): 847–57. doi: 10.1515/bchm2.1984.365.2.847. PMID  6489933.


From Wikipedia, the free encyclopedia
dimethylmaleate hydratase
Identifiers
EC no. 4.2.1.85
CAS no. 93229-56-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme dimethylmaleate hydratase ( EC 4.2.1.85) catalyzes the chemical reaction

(2R,3S)-2,3-dimethylmalate dimethylmaleate + H2O

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (2R,3S)-2,3-dimethylmalate hydro-lyase (dimethylmaleate-forming). This enzyme is also called (2R,3S)-2,3-dimethylmalate hydro-lyase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, iron.

References

  • Kollmann-Koch A, Eggerer H (1984). "Nicotinic acid metabolism. Dimethylmaleate hydratase". Hoppe-Seyler's Z. Physiol. Chem. 365 (8): 847–57. doi: 10.1515/bchm2.1984.365.2.847. PMID  6489933.



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