PMID:3038024: Difference between revisions
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status | !|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status | ||
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[[purA:Gene Product(s)]] | |||
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[[Category:GO:0004019_!_adenylosuccinate_synthase_activity]][http://gowiki.tamu.edu/wiki/index.php/Category:GO:0004019_!_adenylosuccinate_synthase_activity GO:0004019] | |||
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adenylosuccinate synthase activity | |||
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IDA: Inferred from Direct Assay | |||
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F | |||
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PurA (adenylosuccinute synthetase) was purified and assayed for formation of adenylosuccinute per min (Table 1 and Figure 3). | |||
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complete | |||
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[[purA:Gene Product(s)]] | |||
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[[Category:GO:0015949_!_nucleobase,_nucleoside_and_nucleotide_interconversion]][http://gowiki.tamu.edu/wiki/index.php/Category:GO:0015949_!_nucleobase,_nucleoside_and_nucleotide_interconversion GO:0015949] | |||
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nucleobase, nucleoside and nucleotide interconversion | |||
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IDA: Inferred from Direct Assay | |||
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P | |||
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complete | |||
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Revision as of 00:54, 18 November 2008
Bass, MB, Fromm, HJ and Stayton, MM (1987) Overproduction, purification, and characterization of adenylosuccinate synthetase from Escherichia coli.Arch. Biochem. Biophys. 256:335-42
| Abstract | Adenylosuccinate synthetase, encoded by the purA gene of Escherichia coli, catalyzes the first committed step toward AMP in the de novo purine biosynthetic pathway and plays an important role in the interconversion of purines. A 3.2-kb DNA fragment, which carries the purA gene, was cloned into the temperature-inducible, high-copy-number plasmid vector, pMOB45. Upon temperature induction, cells containing this plasmid produce adenylosuccinate synthetase at approximately 40 times the wild-type level. A scheme is presented for the purification of the overproduced adenylosuccinate synthetase to homogeneity in amounts sufficient for studies of its structure and mechanism. The wild-type and the overproduced adenylosuccinate synthetase enzyme preparations were judged to be identical by the following criteria. The amino acid sequence at the N-terminus of the overproduced enzyme proved identical to the corresponding sequence of the wild-type enzyme. Michaelis constants for both the wild-type and overproduced enzyme preparations were the same. And (iii) both proteins shared similar chromatographic behavior and the same mobility during sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. Results from size-exclusion chromatography and SDS-polyacrylamide gel electrophoresis suggest that adenylosuccinate synthetase exists as a dimer of identical, 48,000-Da, subunits. |
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Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004019 |
adenylosuccinate synthase activity |
IDA: Inferred from Direct Assay |
F |
PurA (adenylosuccinute synthetase) was purified and assayed for formation of adenylosuccinute per min (Table 1 and Figure 3). |
complete | |||
| GO:0015949 |
nucleobase, nucleoside and nucleotide interconversion |
IDA: Inferred from Direct Assay |
P |
complete | ||||
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