Intermediate metabolism of aerobic spores. V. The purification and properties of l-alanine dehydrogenase
An l-alanine dehydrogenase (AID) has been purified from extracts of spores of Bacillus cereus strain T. This enzyme catalyzes the reversible reaction: l-alanine + DPN + + H 2O ⇌ pyruvate + NH 3 + DPNH + H + The enzyme is specific for DPN and is inhibited by heavy metals and sulfhydrylbinding agents....
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Veröffentlicht in: | Archives of biochemistry and biophysics 1960-12, Vol.91 (2), p.290-299 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | An
l-alanine dehydrogenase (AID) has been purified from extracts of spores of
Bacillus cereus strain T. This enzyme catalyzes the reversible reaction:
l-alanine + DPN
+ + H
2O ⇌ pyruvate + NH
3 + DPNH + H
+ The enzyme is specific for DPN and is inhibited by heavy metals and sulfhydrylbinding agents. The pH optimum for deamination is 9.8 and for amination 8.8. The equilibrium constant is 1.36 × 10
−14. The properties of the enzyme are identical to those previously described for the AID of vegetative cells of
Bacillus. In spores, AID is the primary route of
l-alanine deamination. |
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ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/0003-9861(60)90503-8 |