Methionine aminopeptidases with short sequence inserts within the catalytic domain are differentially inhibited: Structural and biochemical studies of three proteins from Vibrio spp.-Reference-Cited by-同舟云学术

Methionine aminopeptidases with short sequence inserts within the catalytic domain are differentially inhibited: Structural and biochemical studies of three proteins from Vibrio spp.

Published:2021-01 Issue: Volume:209 Page:112883
ISSN:0223-5234
Container-title:European Journal of Medicinal Chemistry
language:en
Short-container-title:European Journal of Medicinal Chemistry

Author:

Pillalamarri Vijaykumar^ORCID,Reddy Chilakala Gangi,Bala Sandeep Chowdary^ORCID,Jangam Aruna,Kutty Vinny Vinod^ORCID,Addlagatta Anthony^ORCID

Funder

Department of Science and Technology, Ministry of Science and Technology, India

Publisher

Elsevier BV

Subject

Organic Chemistry,Drug Discovery,Pharmacology,General Medicine

Reference61 articles.

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3. Metalloaminopeptidases: common functional themes in disparate structural surroundings;Lowther;Chem. Rev.,2002

4. Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal;Solbiati;J. Mol. Biol.,1999

5. Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes;Arfin;Proc. Natl. Acad. Sci. U. S. A.,1995

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