Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kishimoto, K.; Yoshimura, T.; Esaki, N.; Sugio, S.; Manning, J.M.; Soda, K.
    Role of leucine 201 of thermostable D-amino acid aminotransferase from a thermophile, Bacillus sp. YM-1 (1995), J. Biochem., 117, 691-696.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.21 expression of wild-type, L201A and L201W mutant enzymes in Escherichia coli Bacillus sp. (in: Bacteria)

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.21 L201A 2% of wild-type kcat Bacillus sp. (in: Bacteria)
2.6.1.21 L201W 0.043% of wild-type kcat Bacillus sp. (in: Bacteria)

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.21 additional information L201A and L201W mutant enzymes lose their activity by incubation with D-alanine with biphasic kinetics Bacillus sp. (in: Bacteria)

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.21 0.63
-
2-oxoglutarate pH 8.0, 37°C, wild-type enzyme Bacillus sp. (in: Bacteria)
2.6.1.21 0.67
-
2-oxoglutarate pH 8.0, 37°C, L201W mutant enzyme Bacillus sp. (in: Bacteria)
2.6.1.21 1.2
-
D-alanine pH 8.0, 37°C, L201W mutant enzyme Bacillus sp. (in: Bacteria)
2.6.1.21 1.5
-
D-alanine pH 8.0, 37°C, L201A mutant enzyme Bacillus sp. (in: Bacteria)
2.6.1.21 4.8
-
2-oxoglutarate pH 8.0, 37°C, L201A mutant enzyme Bacillus sp. (in: Bacteria)
2.6.1.21 20
-
D-alanine pH 8.0, 37°C, wild-type enzyme Bacillus sp. (in: Bacteria)

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.21 Bacillus sp. (in: Bacteria)
-
YM-1, thermophile
-
2.6.1.21 Bacillus sp. (in: Bacteria) YM-1
-
YM-1, thermophile
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.21 wild-type, L201A and L201W mutant enzyme, DEAE-toyopearl Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.21 D-alanine + 2-oxoglutarate
-
Bacillus sp. (in: Bacteria) pyruvate + D-glutamate
-
r
2.6.1.21 D-alanine + 2-oxoglutarate
-
Bacillus sp. (in: Bacteria) YM-1 pyruvate + D-glutamate
-
r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.21 0.12
-
D-alanine pH 8.0, 37°C, L201W mutant enzyme Bacillus sp. (in: Bacteria)
2.6.1.21 5.7
-
D-alanine pH 8.0, 37°C, L201A mutant enzyme Bacillus sp. (in: Bacteria)
2.6.1.21 280
-
D-alanine pH 8.0, 37°C, wild-type enzyme Bacillus sp. (in: Bacteria)

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.21 pyridoxal 5'-phosphate wild-type, L201A and L201W mutant enzyme: 0.89, 0.78 and 0.56 mol per mol of subunit, respectively Bacillus sp. (in: Bacteria)