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Volume 139, Issue 11

Purification and characterization of -histidine aminotransferase from nikkomycin-producing Tü901 Free

Abstract

Cell extracts of grown in nikkomycin production media contained an enzyme (HisAT) that transaminated -histidine as the sole amino substrate with pyruvate as the amino group acceptor. HisAT was purified about 190-fold from the crude extract of . The enzyme was determined by gel filtration and SDS-PAGE to be a homodimer with a subunit molecular mass of approximately 45 kDa. The aminotransferase had maximum activity at pH 7·0 and 37 °C. The enzyme was highly specific for -histidine; pyruvate, 2-oxobutyrate, 2-oxovalerate and 2-oxocaproate were used as keto acceptors to about the same extent. The reaction mechanism was ping-pong. The values for -histidine and pyruvate, determined from Lineweaver-Burk plots, were 25 m and 10 m, respectively. Neither cell extracts of non-producing mutants nor extracts of , a species that does not synthesize nikkomycins, showed transaminating activity with a narrow substrate specificity for -histidine as the amino donor. This strongly suggests that the formation of HisAT is essential for nikkomycin production.

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
© Society for General Microbiology 1993
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1993-11-01
2024-04-20
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Purification and characterization of l-histidine aminotransferase from nikkomycin-producing Streptomyces tendae Tü901
Microbiology 139, 2773 (1993); https://doi.org/10.1099/00221287-139-11-2773
/content/journal/micro/10.1099/00221287-139-11-2773
/content/journal/micro/10.1099/00221287-139-11-2773
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