(R)-3-amino-2-methylpropionate—pyruvate transaminase

From Wikipedia, the free encyclopedia
Jump to: navigation, search
(R)-3-amino-2-methylpropionate-pyruvate transaminase
Identifiers
EC number 2.6.1.40
CAS number 37279-00-8
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 (R)-3-amino-2-methylpropionate—pyruvate transaminase (EC 2.6.1.40) is an enzyme that catalyzes the chemical reaction

(R)-3-amino-2-methylpropanoate + pyruvate 2-methyl-3-oxopropanoate + L-alanine

Thus, the two substrates of this enzyme are (R)-3-amino-2-methylpropanoate and pyruvate, whereas its two products are 2-methyl-3-oxopropanoate and L-alanine.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups, the systematic name of this enzyme class is (R)-3-amino-2-methylpropanoate:pyruvate aminotransferase. Other names in common use include D-3-aminoisobutyrate-pyruvate transaminase, beta-aminoisobutyrate-pyruvate aminotransferase, D-3-aminoisobutyrate-pyruvate aminotransferase, D-3-aminoisobutyrate-pyruvate transaminase, (R)-3-amino-2-methylpropionate transaminase, and D-beta-aminoisobutyrate:pyruvate aminotransferase. But some additional information is that this enzyme catalyzed it transamination with L isomer, but D isomer in natural form, inactive as substrate. Also other names of enzymes similar to this contains, L-3-aminoisobutyrate transaminase, beta-aminobutyric transaminase, L-3-aminoisobutyric aminotransferase, and beta-aminoisobutyrate-alpha-ketoglutarate transaminase.[1]

References[edit]

  1. ^ "Kakimoto Y, Kanazawa A, Taniguchi K, Sano I (1968), and Tamaki N, Sakata SF, Matsuda K (2000)
  • Kakimoto Y, Taniguchi K, Sano I (1969). "D-beta-aminoisobutyrate:pyruvate aminotransferase in mammalian liver and excretion of beta-aminoisobutyrate by man". J. Biol. Chem. 244 (2): 335–40. PMID 5773299. 
  • Tamaki N, Sakata SF, Matsuda K (2000). "Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver". Methods Enzymol. 324: 376–89. doi:10.1016/S0076-6879(00)24247-X. PMID 10989446.