Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1993-4-30
|
| pubmed:abstractText |
N-Carbamoyl-D-amino acid amidohydrolase was purified 119-fold, with 36% overall recovery from a cell-free extract of Comamonas sp. E222c. The purified enzyme was homogeneous as judged by SDS/PAGE. The relative molecular mass of the native enzyme was 120,000 and that of the subunit was 40,000. The purified enzyme hydrolyzed various N-carbamoyl-D-amino acids to D-amino acids, ammonia and carbon dioxide. N-Carbamoyl-D-amino acids having hydrophobic groups served as good substrates for the enzyme. The Km and Vmax values for N-carbamoyl-D-phenylalanine were 19.7 mM and 13.1 units/mg, respectively, and those for N-carbamoyl-D-p-hydroxyphenylglycine were 13.1 mM and 0.56 units/mg, respectively. The enzyme strictly recognized the configuration of the substrate and only the D-enantiomer of the N-carbamoyl amino acid was hydrolyzed. The enzyme activity was not significantly affected by N-carbamoyl-L-amino acids and ammonia. The enzyme was sensitive to thiol reagents and did not require metal ions for its activity. The enzyme did not hydrolyze N-carbamoyl-beta-alanine or N-carbamoyl-DL-aspartate suggesting that the enzyme is different from the N-carbamoylamide-hydrolyzing enzymes involved in the pyrimidine degradation pathway. The enzyme did not hydrolyze allantoin and allantoic acid, which are intermediates in purine degradation, N-carbamoylsarcosine and citrulline, suggesting that it is a novel N-carbamoylamide amidohydrolase.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0014-2956
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
212
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
685-91
|
| pubmed:dateRevised |
2007-7-23
|
| pubmed:meshHeading |
pubmed-meshheading:8462543-Amidohydrolases,
pubmed-meshheading:8462543-Amino Acid Sequence,
pubmed-meshheading:8462543-Amino Acids,
pubmed-meshheading:8462543-Cell-Free System,
pubmed-meshheading:8462543-Chromatography, Gel,
pubmed-meshheading:8462543-Chromatography, Ion Exchange,
pubmed-meshheading:8462543-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8462543-Enzyme Stability,
pubmed-meshheading:8462543-Hydrogen-Ion Concentration,
pubmed-meshheading:8462543-Kinetics,
pubmed-meshheading:8462543-Molecular Sequence Data,
pubmed-meshheading:8462543-Pseudomonas,
pubmed-meshheading:8462543-Substrate Specificity,
pubmed-meshheading:8462543-Thermodynamics
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c purification and characterization.
|
| pubmed:affiliation |
Department of Agricultural Chemistry, Kyoto University, Japan.
|
| pubmed:publicationType |
Journal Article
|