NDLI: Biochemical and functional characterizations of tyrosine phosphatases from pathogenic and nonpathogenic mycobacteria: indication of phenyl cyclopropyl methyl-/phenyl butenyl azoles as tyrosine phosphatase inhibitors

Content Provider	Springer Nature Link
Author	Chatterjee, Aditi Pandey, Sapna Singh, Pramod K. Pathak, Navendu Prakash Rai, Niyati Ramachandran, Ravishankar Tripathi, Rama Pati Srivastava, Kishore K.
Copyright Year	2015
Abstract	Tyrosine phosphorylation is one of the most common means of posttranslational modifications which can generate novel recognition motifs for protein interactions and thereafter affecting cellular localization, protein stability, and enzyme activity. Mycobacterium tuberculosis (Mtb) possesses a wide range of signal transduction systems, including two protein tyrosine phosphatases (PtpA and PtpB). Since functional diversities between protein tyrosine phosphatases (PTPases) are illustrated by regulatory domains and subunits, we have characterized the nature of tyrosine phosphatases from slow-grower pathogenic species Mtb and from fast-grower nonpathogenic species Mycobacterium smegmatis (MS). The findings delineate that the enzymes present in MS have significantly lesser phosphatase activity than PTPases of Mtb as evidenced by low K cat/K m of recombinantly expressed proteins. The K cat/K m for Mtb PtpA was 500–1000-fold higher than MS PTPases. We have designed and synthesized phenyl cyclopropyl methyl-/phenyl butenyl azoles which inhibit growth of mycobacteria, in culture and in macrophages. The mechanism of efficacy of these compounds against mycobacteria was identified and suggested that the inhibition may possibly be mediated via the targeting of Mtb tyrosine phosphatase. The results further added that these compounds exclusively inhibit PtpA of Mtb.
Starting Page	7539
Ending Page	7548
Page Count	10
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	99
Issue Number	18
e-ISSN	14320614
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2015-03-10
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Azoles Mycobacteria Tyrosine phosphatase HTS Target Microbiology Microbial Genetics and Genomics Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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

Stereospecificity of myo-inositol hexakisphosphate hydrolysis by a protein tyrosine phosphatase-like inositol polyphosphatase from Megasphaera elsdenii

Biochemical indication of microbial mass changes using ATP and DNA measurement in biological treatment of thiocyanate

Leishmania-based expression systems

Microbial pathogenesis and tyrosine dephosphorylation: surprising'bedfellows'

RETRACTED ARTICLE: Antituberculars which target decaprenylphosphoryl-β-D-ribofuranose 2′-oxidase DprE1: state of art

Strategies used by pathogenic and nonpathogenic mycobacteria to synthesize rrna (1997).

Recent advances in the biochemistry of spinosyns

Highly enantioselective oxidation of phenyl methyl sulfide and its derivatives into optically pure (S)-sulfoxides with Rhodococcus sp. CCZU10-1 in an n-octane–water biphasic system

Rapid identification of target genes for 3-methyl-1-butanol production in Saccharomyces cerevisiae

Biochemical and functional characterizations of tyrosine phosphatases from pathogenic and nonpathogenic mycobacteria: indication of phenyl cyclopropyl methyl-/phenyl butenyl azoles as tyrosine phosphatase inhibitors

Similar Documents

Stereospecificity of myo-inositol hexakisphosphate hydrolysis by a protein tyrosine phosphatase-like inositol polyphosphatase from Megasphaera elsdenii

Biochemical indication of microbial mass changes using ATP and DNA measurement in biological treatment of thiocyanate

Leishmania-based expression systems

Microbial pathogenesis and tyrosine dephosphorylation: surprising'bedfellows'

RETRACTED ARTICLE: Antituberculars which target decaprenylphosphoryl-β-D-ribofuranose 2′-oxidase DprE1: state of art

Strategies used by pathogenic and nonpathogenic mycobacteria to synthesize rrna (1997).

Recent advances in the biochemistry of spinosyns

Highly enantioselective oxidation of phenyl methyl sulfide and its derivatives into optically pure (S)-sulfoxides with Rhodococcus sp. CCZU10-1 in an n-octane–water biphasic system

Rapid identification of target genes for 3-methyl-1-butanol production in Saccharomyces cerevisiae

Biochemical and functional characterizations of tyrosine phosphatases from pathogenic and nonpathogenic mycobacteria: indication of phenyl cyclopropyl methyl-/phenyl butenyl azoles as tyrosine phosphatase inhibitors