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Literature summary for 3.5.1.6 extracted from

  • Lundgren, S.; Gojkovic, Z.; Piskur, J.; Dobritzsch, D.
    Yeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases (2003), J. Biol. Chem., 278, 51851-51862.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
overexpressed native and selenomethionine-substituted SkbetaAS, hanging drop vapor diffusion method Lachancea kluyveri

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ contains two Zn2+ per subunit, dizinc metal center in the catalytic domain of the subunit representing the active site of enzyme, binding mode Lachancea kluyveri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-methyl-N-carbamoyl-beta-alanine + H2O Lachancea kluyveri betaAS is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of the pyrimidine bases uracil and thymine 2-methyl-beta-alanine + CO2 + NH3
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N-carbamoyl-beta-alanine + H2O Lachancea kluyveri betaAS is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of the pyrimidine bases uracil and thymine beta-alanine + CO2 + NH3
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Organism

Organism UniProt Comment Textmining
Lachancea kluyveri Q96W94
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Purification (Commentary)

Purification (Comment) Organism
recombinant SkbetaAS Lachancea kluyveri

Reaction

Reaction Comment Organism Reaction ID
3-ureidopropanoate + H2O = beta-alanine + CO2 + NH3 detailed reaction mechanism, catalytic mechanism Lachancea kluyveri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-methyl-N-carbamoyl-beta-alanine + H2O betaAS is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of the pyrimidine bases uracil and thymine Lachancea kluyveri 2-methyl-beta-alanine + CO2 + NH3
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?
2-methyl-N-carbamoyl-beta-alanine + H2O catalytic mechanism, substrate-binding residues Lachancea kluyveri 2-methyl-beta-alanine + CO2 + NH3
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additional information detailed enzyme/active site structure, a subunit consists of two domains: a larger catalytic domain with a dizinc metal center representing the active site, and a smaller domain mediating the majority of the intersubunit contacts, conformational changes occur during each catalytic cycle Lachancea kluyveri ?
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?
N-carbamoyl-beta-alanine + H2O betaAS is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of the pyrimidine bases uracil and thymine Lachancea kluyveri beta-alanine + CO2 + NH3
-
?
N-carbamoyl-beta-alanine + H2O catalytic mechanism, substrate-binding residues Lachancea kluyveri beta-alanine + CO2 + NH3
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?

Subunits

Subunits Comment Organism
homodimer a subunit of the homodimer consists of two domains: a larger catalytic domain with a dizinc metal center, representing the active site, and a smaller domain mediating the majority of the intersubunit contacts, the dimeric state is essential for catalytic activity Lachancea kluyveri

Synonyms

Synonyms Comment Organism
betaAS
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Lachancea kluyveri
SkbetaAS Saccharomyces kluyveri betaAS Lachancea kluyveri