ENZYME DISTRIBUTION AS A FACTOR IN THE INDEPENDENCE OF BACILLUS CEREUS SPORE GERMINATION FROM L- AND D-CYSTEINE DESULFHYDRASE ACTIVITY

Abstract

The release of H2S, pyruvate, and NH3 from L- and D-cysteine by extracts from B. cereus strain T spores is ascribed to the mediation of specific L- and D-cysteine desulfhydrases. D-isomer activity is differentiated by pyridoxal phosphate independence, five-fold greater activity, and relative resistance to inhibition by semicarbazide. Inhibition by NH2OH does not permit differentiation. Low recoveries of pyruvate (26 to 47%) are associated with a nonenzymic reaction between pyruvate and L- or D-cysteine.

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Document Details

Document Type
Technical Report
Publication Date
Dec 01, 1965
Accession Number
AD0476395

Entities

People

  • Bernard J. Krask
  • George E. Fulk

Organizations

  • United States Army Biological Warfare Laboratories

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Acids
  • Alanine
  • Amino Acids
  • Biological Laboratories
  • Butyric Acids
  • Carboxylic Acids
  • Cysteine
  • Escherichia Coli
  • Germination
  • Inhibition
  • Inhibitors
  • Pyridoxal Phosphate
  • Pyruvates
  • Recovery
  • Semicarbazides
  • United States
  • United States Government

Fields of Study

  • Biology

Readers

  • Mathematics or Statistics
  • Military/Explosive Ordnance Disposal (EOD) Technology
  • Molecular and Cellular Biochemistry