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A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study.

Authors
  • Munier-Lehmann, H
  • Burlacu-Miron, S
  • Craescu, C T
  • Mantsch, H H
  • Schultz, C P
Type
Published Article
Journal
Proteins: Structure, Function, and Bioinformatics
Publisher
Wiley
Publication Date
Aug 01, 1999
Volume
36
Issue
2
Pages
238–248
Identifiers
PMID: 10398370
Source
Medline
License
Unknown

Abstract

The adk gene from Mycobacterium tuberculosis codes for an enzyme of 181 amino acids. A sequence comparison with 52 different forms of adenylate kinases (AK) suggests that the enzyme from M. tuberculosis belongs to a new subfamily of "short" bacterial AKs. The recombinant protein, overexpressed in Escherichia coli, exhibits a low catalytic activity and an unexpectedly high thermal stability (Tm = 64.8 degrees C). Based on various spectroscopic data, on the known three-dimensional structure of the AK from E. coli and on secondary structure predictions for various sequenced AKs, we propose a structural model for AK from M. tuberculosis (AKmt). Proteins 1999;36:238-248.

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