Crystal structure of X‐prolyl aminopeptidase from Caenorhabditis elegans : A cytosolic enzyme with a di‐nuclear active site-Reference-Cited by-同舟云学术

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Crystal structure of X‐prolyl aminopeptidase from Caenorhabditis elegans : A cytosolic enzyme with a di‐nuclear active site

Published:2015-01 Issue:1 Volume:5 Page:292-302
ISSN:2211-5463
Container-title:FEBS Open Bio
language:en
Short-container-title:FEBS Open Bio

Author:

Iyer Shalini¹,La-Borde Penelope J.¹²,Payne Karl A.P.³⁴,Parsons Mark R.³⁵,Turner Anthony J.³,Isaac R. Elwyn³,Acharya K. Ravi¹

Affiliation:

1. Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK

2. School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK

3. Faculty of Biological Sciences, Clarendon Way, University of Leeds, Leeds LS2 9JT, UK

4. Faculty of Life Sciences, University of Manchester, Manchester M13 9PL, UK

5. Sevenoaks School, Sevenoaks TN13 1HU, UK

Publisher

Wiley

Subject

General Biochemistry, Genetics and Molecular Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1016/j.fob.2015.03.013

Reference57 articles.

1. Catalytic Mechanisms for Metallopeptidases

2. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

3. Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.

4. Proline motifs in peptides and their biological processing

5. Proline specific endo- and exopeptidases

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2. Proline-specific aminopeptidase P prevents replication-associated genome instability;PLOS Genetics;2022-01-26

3. Structure-Function and Industrial Relevance of Bacterial Aminopeptidase P;Catalysts;2021-09-26

4. Intrinsically disordered protein PID‐2 modulates Z granules and is required for heritable piRNA‐induced silencing in the Caenorhabditis elegans embryo;The EMBO Journal;2020-11-24

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