Crystallization (Comment) | Organism |
---|---|
overexpressed native and selenomethionine-substituted SkbetaAS, hanging drop vapor diffusion method | Lachancea kluyveri |
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 | 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 | - |
? | |
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 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lachancea kluyveri | Q96W94 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant SkbetaAS | Lachancea kluyveri |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
3-ureidopropanoate + H2O = beta-alanine + CO2 + NH3 | detailed reaction mechanism, catalytic mechanism | Lachancea kluyveri |
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 | - |
? | |
2-methyl-N-carbamoyl-beta-alanine + H2O | catalytic mechanism, substrate-binding residues | Lachancea kluyveri | 2-methyl-beta-alanine + CO2 + NH3 | - |
? | |
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 | ? | - |
? | |
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 | - |
? |
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 | Comment | Organism |
---|---|---|
betaAS | - |
Lachancea kluyveri |
SkbetaAS | Saccharomyces kluyveri betaAS | Lachancea kluyveri |