Mycobacterium tuberculosis histidinol dehydrogenase: biochemical characterization and inhibition studies

RSC Advances ◽  
2016 ◽  
Vol 6 (34) ◽  
pp. 28406-28418 ◽  
Author(s):  
Juleane Lunardi ◽  
Leonardo Kras Borges Martinelli ◽  
Alessandra Silva Raupp ◽  
José Eduardo Sacconi Nunes ◽  
Diana Carolina Rostirolla ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Biochemical Characterization ◽  
Biochemical Studies ◽  
Histidinol Dehydrogenase ◽  
Inhibition Studies

We describe a series of biochemical studies on recombinantMycobacterium tuberculosisHisD (MtHisD) and the synthesis of a series of compounds which are, to the best of our knowledge, the first inhibitors ofMtHisD activity reported in the literature.

scholarly journals Biochemical characterization and zinc binding group (ZBGs) inhibition studies on the catalytic domain of MMP7 (cdMMP7)

2016 ◽  
Vol 165 ◽  
pp. 7-17 ◽  
Author(s):  
Fan Meng ◽  
Hao Yang ◽  
Colin Jack ◽  
Huaqun Zhang ◽  
Abraham Moller ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Catalytic Domain ◽  
Zinc Binding ◽  
Inhibition Studies

scholarly journals Brucella suis histidinol dehydrogenase: Synthesis and inhibition studies of substituted N-L-histidinylphenylsulfonyl hydrazide

2008 ◽  
Vol 23 (3) ◽  
pp. 357-361 ◽  
Author(s):  
Marie-Rose Abdo ◽  
Pascale Joseph ◽  
Rose-Anne Boigegrain ◽  
Jean-Louis Montero ◽  
Stephan Köhler ◽  
...  
Keyword(s):  
Brucella Suis ◽  
Histidinol Dehydrogenase ◽  
Inhibition Studies

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.

The RD1 proteins of Mycobacterium tuberculosis: expression in Mycobacterium smegmatis and biochemical characterization

2003 ◽  
Vol 5 (12) ◽  
pp. 1082-1095 ◽  
Author(s):  
Sabine Daugelat ◽  
Jane Kowall ◽  
Jens Mattow ◽  
Dirk Bumann ◽  
Ralf Winter ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Mycobacterium Smegmatis ◽  
Biochemical Characterization

scholarly journals Understanding the Role of PknJ in Mycobacterium tuberculosis: Biochemical Characterization and Identification of Novel Substrate Pyruvate Kinase A

PLoS ONE ◽  
2010 ◽  
Vol 5 (5) ◽  
pp. e10772 ◽  
Author(s):  
Gunjan Arora ◽  
Andaleeb Sajid ◽  
Meetu Gupta ◽  
Asani Bhaduri ◽  
Pawan Kumar ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Pyruvate Kinase ◽  
Biochemical Characterization ◽  
Kinase A

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.

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