| Predicate | Object |
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Adenylosuccinate synthetase
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| http://www.biopax.org/relea... |
PURA_YEAST
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
6.3.4.4,
AMPSase,
AS-synthetase,
AdSS,
IMP--aspartate ligase
|
| http://www.biopax.org/relea... |
FUNCTION: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP. CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. COFACTOR: Binds 1 magnesium ion per subunit (By similarity). ENZYME REGULATION: Inhibited by GMP. Inhibited by chloride. Inhibited in a highly specific manner by the binding of a 44-base DNA oligonucleotide carrying the ARS core consensus sequence. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1650 uM for L-aspartate; KM=200 uM for IMP; KM=1650 uM for GTP; pH dependence: Optimum pH is 8.0; Temperature dependence: Optimum temperature is 35 degrees Celsius; PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Cytoplasm. MISCELLANEOUS: Present with 56800 molecules/cell in log phase SD medium. SIMILARITY: Belongs to the adenylosuccinate synthetase family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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