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Literature summary for 2.6.1.21 extracted from

  • Soper, T.S.; Manning, J.M.; Marcotte, P.A.; Walsh, C.T.
    Inactivation of bacterial D-amino acid transaminases by the olefinic amino acid D-vinylglycine (1977), J. Biol. Chem., 252, 1571-1575.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-Amino-3-butenoate D-alanine in a 10fold excess over vinylglycin affords a 70% protection against inactivation; i.e. vinylglycine, little if any inactivation in absence of 2-oxoglutarate as cosubstrate, in presence of 2-oxoglutarate pseudo-first order kinetics inactivation, inactivation mechanism Bacillus subtilis
2-Amino-3-butenoate i.e. vinylglycine, little if any inactivation in absence of 2-oxoglutarate as cosubstrate, in presence of 2-oxoglutarate pseudo-first order kinetics inactivation, inactivation mechanism Lysinibacillus sphaericus

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Lysinibacillus sphaericus
-
-
-

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate a pyridoxal phosphate protein Bacillus subtilis
pyridoxal 5'-phosphate a pyridoxal phosphate protein Lysinibacillus sphaericus