Adenylate Kinase Activity in Mycobacterium leprae
- 1 February 1986
- journal article
- research article
- Published by Microbiology Society in Microbiology
- Vol. 132 (2) , 561-563
- https://doi.org/10.1099/00221287-132-2-561
Abstract
Adenylate kinase (ATP:AMP phsophotransferase, EC 2.7.4.3) was detected in partially purified preparations of cell-free extracts of Mycobacterium leprae. The apparent Km values of M. leprae adenylate kinase for ADP and Mg2+ were 1 .times. 10-4 M and 4 .times. 10-4 M, respectively. The enzyme was heat-liable: loss of activity by 80% at 45.degree. C and over 90% at 60.degree. C occurred within 5 min. M. leprae adenylate kinase was distinct from armadillo adenylate kinase in respect of affinity for substrate and heat-sensitivity.This publication has 6 references indexed in Scilit:
- Measurement of ATP Generation and Decay in Mycobacterium leprae in vitroMicrobiology, 1985
- Oxidation of Carbon Sources through the Tricarboxylic Acid Cycle in Mycobacterium leprae Grown in Armadillo LiverMicrobiology, 1984
- Catabolic Pathways for Glucose, Glycerol and 6-Phosphogluconate in Mycobacterium leprae grown in Armadillo TissuesMicrobiology, 1983
- Adenine nucleotide and lysine transport in Chlamydia psittaciJournal of Bacteriology, 1982
- N-Acetyl- -glucosaminidase, -Glucuronidase and Acid Phosphatase in Mycobacterium lepraeMicrobiology, 1982
- Preliminary Studies of the Metabolic Activity of Purified Suspensions of Mycobacterium lepraeMicrobiology, 1982