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Literature summary for 2.6.1.1 extracted from

  • Son, H.; Kim, K.
    Structural insights into a novel class of aspartate aminotransferase from Corynebacterium glutamicum (2016), PLoS ONE, 11, e0158402.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Corynebacterium glutamicum

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with pyridoxal phosphate and a citrate molecule, to 2.0 A resolution Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
D220A mutation in pyridoxal phosphate-binding residue, almost complete loss of activity Corynebacterium glutamicum
K259A mutation in pyridoxal phosphate-binding residue, almost complete loss of activity Corynebacterium glutamicum
K41A mutation in substrate-binding residue, about 60% of wild-type activity Corynebacterium glutamicum
N191A mutation in pyridoxal phosphate-binding residue, almost complete loss of activity Corynebacterium glutamicum
R144A mutation in substrate-binding residue, about 25% of wild-type activity Corynebacterium glutamicum
R394A mutation in substrate-binding residue, almost complete loss of activity Corynebacterium glutamicum
R39A mutation in substrate-binding residue, almost complete loss of activity Corynebacterium glutamicum
S103A mutation in pyridoxal phosphate-binding residue, about 70% of wild-type activity Corynebacterium glutamicum
S104A mutation in pyridoxal phosphate-binding residue, about 70% of wild-type activity Corynebacterium glutamicum
S258A mutation in pyridoxal phosphate-binding residue, about 80% of wild-type activity Corynebacterium glutamicum
Y142A mutation in pyridoxal phosphate-binding residue, almost complete loss of activity Corynebacterium glutamicum
Y223A mutation in pyridoxal phosphate-binding residue, almost complete loss of activity Corynebacterium glutamicum
Y73A almost complete loss of activity Corynebacterium glutamicum

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q8NTR2
-
-
Corynebacterium glutamicum ATCC 13032 Q8NTR2
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
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Corynebacterium glutamicum oxaloacetate + L-glutamate
-
?
L-aspartate + 2-oxoglutarate
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Corynebacterium glutamicum ATCC 13032 oxaloacetate + L-glutamate
-
?

Synonyms

Synonyms Comment Organism
Cgl0240
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Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate tight binding to the enzyme, enzyme exhibits catalytic activity without the addition of pyridoxal phosphate to the reaction mixture. The pyridoxal ring is stabilized by the hydrogen bonds with residues Tyr142, Asn191, Asp220, Tyr223, and Lys259 Corynebacterium glutamicum