Biochemical characterization of Mycobacterium tuberculosis IMP dehydrogenase: kinetic mechanism, metal activation and evidence of a cooperative system

RSC Advances ◽  
2014 ◽  
Vol 4 (50) ◽  
pp. 26271-26287 ◽  
Author(s):  
Diana Carolina Rostirolla ◽  
Thiago Milech de Assunção ◽  
Cristiano Valim Bizarro ◽  
Luiz Augusto Basso ◽  
Diogenes Santiago Santos
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Biochemical Characterization ◽  
Kinetic Mechanism ◽  
Cooperative System ◽  
Imp Dehydrogenase ◽  
System P

Proposed kinetic mechanism for MtIMPDH in the presence of K+.

Biochemical Characterization of VapC46 Toxin from Mycobacterium tuberculosis

2020 ◽  
Vol 62 (6-7) ◽  
pp. 335-343
Author(s):  
Madhurima Roy ◽  
Madhuparna Bose ◽  
Kamakshi Bankoti ◽  
Anirban Kundu ◽  
Santanu Dhara ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Biochemical Characterization

scholarly journals Evidence for an Elongated Dimeric Structure of Heparin-Binding Hemagglutinin from Mycobacterium tuberculosis

2008 ◽  
Vol 190 (13) ◽  
pp. 4749-4753 ◽  
Author(s):  
Carla Esposito ◽  
Maxim V. Pethoukov ◽  
Dmitri I. Svergun ◽  
Alessia Ruggiero ◽  
Carlo Pedone ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Virulence Factor ◽  
Biochemical Characterization ◽  
Coiled Coil ◽  
Heparin Binding ◽  
Truncated Form ◽  
X Ray ◽  
Dimeric Structure ◽  
X Ray Scattering

ABSTRACT Heparin-binding hemagglutinin (HBHA) is a virulence factor of tuberculosis which is responsible for extrapulmonary dissemination of this disease. A thorough biochemical characterization of HBHA has provided experimental evidence of a coiled-coil nature of HBHA. These data, together with the low-resolution structures of a full-length form and a truncated form of HBHA obtained by small-angle X-ray scattering, have unambiguously indicated that HBHA has a dimeric structure with an elongated shape.

Biochemical characterization of an S-adenosyl-l-methionine-dependent methyltransferase (Rv0469) of Mycobacterium tuberculosis

2013 ◽  
Vol 394 (7) ◽  
pp. 871-877 ◽  
Author(s):  
Laxman S. Meena ◽  
Puneet Chopra ◽  
Ram A. Vishwakarma ◽  
Yogendra Singh
Keyword(s):  
Fatty Acids ◽  
Mycobacterium Tuberculosis ◽  
Oleic Acid ◽  
Biochemical Characterization ◽  
Short Chain Fatty Acids ◽  
Major Constituent ◽  
Membrane Phospholipids ◽  
Tuberculostearic Acid ◽  
Olefinic Double Bond

Abstract Tuberculostearic acid (l0-methylstearic acid, TSA) is a major constituent of mycobacterial membrane phospholipids, and its biosynthesis involves the direct methylation of oleic acid esterified as a component of phospholipids. The methyltransferases of mycobacteria were long proposed to be involved in the synthesis of methyl-branched short-chain fatty acids, but direct experimental evidence is still lacking. In this study, we identified the methyltransferase encoded by umaA in Mycobacterium tuberculosis H37Rv as a novel S-adenosyl-l-methionine (SAM)-dependent methyltransferase capable of catalyzing the conversion of olefinic double bond of phospholipid-linked oleic acid to biologically essential TSA. Therefore, UmaA, catalyzing such modifications, offer a viable target for chemotherapeutic intervention.

Biochemical characterization of Mycobacterium tuberculosis LexA and structural studies of its C-terminal segment

2019 ◽  
Vol 75 (1) ◽  
pp. 41-55
Author(s):  
A. V. Chandran ◽  
R. Srikalaivani ◽  
A. Paul ◽  
M. Vijayan
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Cleavage Site ◽  
Biochemical Characterization ◽  
Terminal Segment ◽  
Full Length ◽  
Mutual Orientation ◽  
Crystal Formation ◽  
Wild Type ◽  
Catalytic Core

LexA is a protein that is involved in the SOS response. The protein from Mycobacterium tuberculosis and its mutants have been biochemically characterized and the structures of their catalytic segments have been determined. The protein is made up of an N-terminal segment, which includes the DNA-binding domain, and a C-terminal segment encompassing much of the catalytic domain. The two segments are defined by a cleavage site. Full-length LexA, the two segments, two point mutants involving changes in the active-site residues (S160A and K197A) and another mutant involving a change at the cleavage site (G126D) were cloned and purified. The wild-type protein autocleaves at basic pH, while the mutants do not. The wild-type and the mutant proteins dimerize and bind DNA with equal facility. The C-terminal segment also dimerizes, and it also shows a tendency to form tetramers. The C-terminal segment readily crystallized. The crystals obtained from attempts involving the full-length protein and its mutants contained only the C-terminal segment including the catalytic core and a few residues preceding it, in a dimeric or tetrameric form, indicating protein cleavage during the long period involved in crystal formation. Modes of tetramerization of the full-length protein similar to those observed for the catalytic core are feasible. A complex of M. tuberculosis LexA and the cognate SOS box could be modeled in which the mutual orientation of the two N-terminal domains differs from that in the Escherichia coli LexA–DNA complex. These results represent the first thorough characterization of M. tuberculosis LexA and provide definitive information on its structure and assembly. They also provide leads for further exploration of this important protein.

scholarly journals Biochemical characterization of the Mycobacterium tuberculosis phosphoribosyl-1-pyrophosphate synthetase

Glycobiology ◽  
2010 ◽  
Vol 21 (4) ◽  
pp. 410-425 ◽  
Author(s):  
L. J. Alderwick ◽  
G. S. Lloyd ◽  
A. J. Lloyd ◽  
A. L. Lovering ◽  
L. Eggeling ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Biochemical Characterization
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