S1 pocket fingerprints of human and bacterial methionine aminopeptidases determined using fluorogenic libraries of substrates and phosphorus based inhibitors

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F12%3A00376236" target="_blank" >RIV/61388963:_____/12:00376236 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1016/j.biochi.2011.10.014" target="_blank" >http://dx.doi.org/10.1016/j.biochi.2011.10.014</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.biochi.2011.10.014" target="_blank" >10.1016/j.biochi.2011.10.014</a>

Result language

angličtina

Original language name

S1 pocket fingerprints of human and bacterial methionine aminopeptidases determined using fluorogenic libraries of substrates and phosphorus based inhibitors

Original language description

Methionyl aminopeptidases (MetAPs) are metallo-dependent proteases responsible for removing of N-terminal methionine residue of peptides and proteins during protein maturation and activation. In this report we use a comprehensive strategy to screen the substrate specificity of three methionyl aminopeptidases: Homo sapiens MetAP-1, Homo sapiens MetAP-2 and Escherichia coli MetAP-1. By utilizing a 65-membered fluorogenic substrate library consisting of natural and unnatural amino acids we established detailed substrate preferences of each enzyme in the S1 pocket. Our results show that this pocket is highly conserved for all investigated MetAPs, very stringent for methionine, and that several unnatural amino acids with methionine-like characteristics werealso well hydrolyzed by MetAPs. The substrate-derived results were verified using several phosphonate and phosphinate-based inhibitors.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CC - Organic chemistry

OECD FORD branch

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Project

<a href="/en/project/LC06077" target="_blank" >LC06077: Center of Chemical Genetics</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2012

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochimie

ISSN

0300-9084

e-ISSN

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Volume of the periodical

94

Issue of the periodical within the volume

3

Country of publishing house

FR - FRANCE

Number of pages

7

Pages from-to

704-710

UT code for WoS article

000301332200014

EID of the result in the Scopus database

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