Variations in the pathways of malate oxidation and phosphorylation in different species of Mycobacteria

Biochim Biophys Acta. 1975 Feb 17;376(2):210-8. doi: 10.1016/0005-2728(75)90012-2.

Abstract

Mycobacterium tuberculosis H37Rv, the slow-growing human pathogenic strain of tubercle bacilli and Mycobacterium smegmatis and Mycobacterium phlei, the fast-growing saprophytes, have shown variations regarding the type of dehydrogenase that initiates malate oxidation in the respiratory chain. M. tuberculosis H37Rv is characterized by having a malate oxidase system (designated MALNAD pathway) in which malate oxidation is mediated by the NAD+-dependent malate dehydrogenase (EC 1.1.1.37) but not by FAD-dependent malate-vitamin K reductase. M. smegmatis possesses a different malate oxidase system (designated MALFAD pathway) in which malate oxidation is exclusively carried out by the FAD-dependent malate-vitamin K reductase because NAD+-dependent malate dehydrogenase is absent in this organism. M. phlei has a mixed system of malate oxidase (designated MALNAD+FAD pathways) in which both the NAD+-and FAD-dependent dehydrogenases take part. In all the three systems, the rest of the electron transport chain is common.

MeSH terms

  • Alcohol Oxidoreductases / metabolism
  • Flavin-Adenine Dinucleotide
  • Genetic Variation
  • Malate Dehydrogenase / metabolism
  • Malates / metabolism*
  • Mycobacterium / metabolism*
  • Mycobacterium tuberculosis / metabolism
  • NAD
  • Oxidative Phosphorylation*
  • Oxygen Consumption
  • Species Specificity
  • Spectrophotometry
  • Succinate Dehydrogenase / metabolism
  • Vitamin K

Substances

  • Malates
  • NAD
  • Vitamin K
  • Flavin-Adenine Dinucleotide
  • Alcohol Oxidoreductases
  • Malate Dehydrogenase
  • Succinate Dehydrogenase