NDLI: Structural and functional investigation into acetyl-coenzyme A synthase and methyltransferase from human pathogen Clostridium difficile

Please wait, while we are loading the content...

A coupling system of capillary gel electrophoresis with inductively coupled plasma-mass spectrometry for the determination of double stranded DNA fragments

Analysis of animal and plant selenometabolites in roots of a selenium accumulator, Brassica rapa var. peruviridis, by speciation

Suppression of ZIP8 expression is a common feature of cadmium-resistant and manganese-resistant RBL-2H3 cells

Selenium metabolism and excretion in mice after injection of ⁸²Se-enriched selenomethionine

d-Histidine and l-histidine attenuate zinc-induced neuronal death in GT1-7 cells

Synthesis of antitumor azolato-bridged dinuclear platinum(ii) complexes with in vivo antitumor efficacy and unique in vitro cytotoxicity profiles

The role of glutathione in the metabolism of diphenylarsinic acid in rats

Elevated amyloid-β plaque deposition in dietary selenium-deficient Tg2576 transgenic mice

AMP-activated protein kinase-mediated glucose transport as a novel target of tributyltin in human embryonic carcinoma cells

Scanning protein analysis of electrofocusing gels using X-ray fluorescence

Evaluation of quantitative probes for weaker Cu(i) binding sites completes a set of four capable of detecting Cu(i) affinities from nanomolar to attomolar

A platinum complex that binds non-covalently to DNA and induces cell death via a different mechanism than cisplatin

Bioeffects of a combination of trace elements on adipocyte biology

The early molecular processes underlying the neurological manifestations of an animal model of Wilson's disease

Comparative proteomics analysis of sodium selenite-induced apoptosis in human prostate cancer cells

Structural and functional investigation into acetyl-coenzyme A synthase and methyltransferase from human pathogen Clostridium difficile

Back cover

Metallomics Vol - 5 Issue - 4

Metallomics Vol - 5 Issue - 3

Metallomics Vol - 5 Issue - 2

Structural and functional investigation into acetyl-coenzyme A synthase and methyltransferase from human pathogen Clostridium difficile

Content Provider	Royal Society of Chemistry (RSC)
Author	Zhu, Xiaofei Zhang, Sixue Wang, Yu Liu, Yi Tan, Xiangshi Li, Tiejun Gu, Xiang
Copyright Year	2013
Abstract	Methyltransferase (MeTrCd) and acetyl-coenzyme A synthase (ACSCd) are two key enzymes in the acetyl-coenzyme A synthesis pathway of the human pathogen Clostridium difficile. The pathway is absent in humans and is essential for the survival of the pathogen. MeTrCd and ACSCd were cloned, expressed in E. coli, and characterized for the first time. Structural and functional investigations of the two enzymes were performed using homology structure modeling, fluorescence spectroscopy, and steady state/pre-steady state kinetics. The conformational change and methyl transfer activity of MeTrCd were shown to be pH dependent. The kinetic studies of MeTrCd at the optimal pH 5.1 yield the parameters kcat (2.63 s−1), Km (17.8 μM) and kcat/Km (0.15 μM−1 s−1). The active site metal cluster (A-cluster) of ACSCd, [Fe4S4][NipNid], was characterized using metal analysis, structural modeling, and UV/Vis spectra of the characteristic features of [Fe4S4] cubane. Nip, as a labile metal, can be removed by treatment with chelators, resulting in the loss of ACS activity. Three bidentate chelators (1,10-phenanthroline, 8-hydroxyquinoline, and 2,2-dipyridyl) exhibited excellent inhibition effects on ACSCd methyl group transfer and acetyl-coenzyme A synthesis activity. These inhibitory effects were further examined using antibacterial activity assays against Clostridium difficile. These results provide a new strategy to find new potential antibiotics for the treatment of CDI.
Starting Page	551
Ending Page	558
Page Count	8
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	5
Issue Number	5
Journal	Metallomics
DOI	10.1039/c3mt20257g
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Clostridium 8-Hydroxyquinoline Spectroscopy Escherichia coli Active site Methyltransferase Specificity constant Fluorescence CDI Acetyl-CoA Sequence homology ACS Methyl group Denticity PH Cluster chemistry Willem C. Vis Moot Cubane Phenanthroline Pathogen
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Theoretical Studies of Acetyl-CoA Synthase Catalytic Mechanism

Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase.

Isolation of the acetyl-coa synthase gene from the corn smut pathogen, ustilago maydis (1989).

Solvent effect on the UV/Vis absorption and fluorescence spectroscopic properties of berberine

Equilibrium dialysis study and mechanistic implications of coenzyme A binding to acetyl-CoA synthase/carbon monoxide dehydrogenase from Clostridium thermoaceticum

Willem C. Vis International Commercial Arbitration Moot

Porphyrin–hexaphyrin hybrid tapes

Equilibrium dialysis study and mechanistic implications of coenzyme A binding to acetyl-CoA synthase/carbon monoxide dehydrogenase from Clostridium thermoaceticum

Editorial: The Deadly Secrets of C. difficile—Insights Into Host-Pathogen Interaction

Structural and functional investigation into acetyl-coenzyme A synthase and methyltransferase from human pathogen Clostridium difficile

Similar Documents

Theoretical Studies of Acetyl-CoA Synthase Catalytic Mechanism

Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase.

Isolation of the acetyl-coa synthase gene from the corn smut pathogen, ustilago maydis (1989).

Solvent effect on the UV/Vis absorption and fluorescence spectroscopic properties of berberine

Equilibrium dialysis study and mechanistic implications of coenzyme A binding to acetyl-CoA synthase/carbon monoxide dehydrogenase from Clostridium thermoaceticum

Willem C. Vis International Commercial Arbitration Moot

Porphyrin–hexaphyrin hybrid tapes

Equilibrium dialysis study and mechanistic implications of coenzyme A binding to acetyl-CoA synthase/carbon monoxide dehydrogenase from Clostridium thermoaceticum

Editorial: The Deadly Secrets of C. difficile—Insights Into Host-Pathogen Interaction

Structural and functional investigation into acetyl-coenzyme A synthase and methyltransferase from human pathogen Clostridium difficile