Methylaspartate mutase

From Wikipedia, the free encyclopedia
Jump to: navigation, search
methylaspartate mutase
Identifiers
EC number 5.4.99.1
CAS number 9032-97-7
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

In enzymology, a methylaspartate mutase (EC 5.4.99.1) is an enzyme that catalyzes the chemical reaction

L-threo-3-methylaspartate L-glutamate

Hence, this enzyme has one substrate, L-threo-3-methylaspartate, and one product, L-glutamate.

This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is L-threo-3-methylaspartate carboxy-aminomethylmutase. Other names in common use include glutamate mutase, glutamic mutase, glutamic isomerase, glutamic acid mutase, glutamic acid isomerase, methylaspartic acid mutase, beta-methylaspartate-glutamate mutase, and glutamate isomerase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, cobamide.

Structural studies[edit]

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1B1A, 1BE1, 1CB7, 1CCW, 1FMF, 1I9C, 1ID8, and 2PWH.

References[edit]

  • BARKER HA, ROOZE V, SUZUKI F, IODICE AA (1964). "THE GLUTAMATE MUTASE SYSTEM. ASSAYS AND PROPERTIES". J. Biol. Chem. 239: 3260–6. PMID 14245371. 
  • Weissbach H, Toohey J, Barker HA (1959). "Isolation and properties of B12 coenzymes containing benzimidazole or dimethylbenzimidazole". Proc. Natl. Acad. Sci. USA. 45 (4): 521–528. doi:10.1073/pnas.45.4.521.