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Literature summary for 3.5.1.6 extracted from

  • Lundgren, S.; Andersen, B.; Piskur, J.; Dobritzsch, D.
    Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements (2007), J. Biol. Chem., 282, 36037-36047.
    View publication on PubMed
Search for more literature for 3.5.1.6

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of wild-type beta-alanine synthase in complex with the reaction product beta-alanine, and of the mutant E159A with the substrate N-carbamyl-beta-alanine Lachancea kluyveri

Protein Variants

Protein Variants Comment Organism
E159A 0.09% of the wild-type activity Lachancea kluyveri
E159D 0.09% of the wild-type activity Lachancea kluyveri
H226E no activity Lachancea kluyveri
H262A 8.9% of the wild-type activity Lachancea kluyveri
H397N 7.2% of the wild-type activity Lachancea kluyveri
R322A 0.14% of the wild-type activity Lachancea kluyveri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
60
-
 N-Carbamoyl-beta-alanine wild-type enzyme Lachancea kluyveri

Organism

Organism UniProt Comment Textmining
Lachancea kluyveri Q96W94
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-carbamoyl-beta-alanine + H2O
-
 Lachancea kluyveri beta-alanine + CO2 + NH3
-
 ?

Synonyms

Synonyms Comment Organism
beta-alanine synthase
-
 Lachancea kluyveri

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.005
-
 N-Carbamoyl-beta-alanine mutant enzyme E159A Lachancea kluyveri
0.005
-
 N-Carbamoyl-beta-alanine mutant enzyme E159D Lachancea kluyveri
0.0077
-
 N-Carbamoyl-beta-alanine mutant enzyme R322A Lachancea kluyveri
0.38
-
 N-Carbamoyl-beta-alanine mutant enzyme H397N Lachancea kluyveri
0.47
-
 N-Carbamoyl-beta-alanine mutant enzyme H262A Lachancea kluyveri
5.3
-
 N-Carbamoyl-beta-alanine wild-type enzyme Lachancea kluyveri