Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F05%3A00022006" target="_blank" >RIV/61388971:_____/05:00022006 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates

Original language description

Detailed biochemical studies were performed with eukaryotic-type serine/threonine protein kinase StkP and phosphoprotein phosphatase PhpP of Streptococcus pneumoniae. Analysis of phosphoproteome maps of both wild type and stkP null mutant strains revealed two possible substrates for StkP. The evidence is presented that StkP can phosphorylate in vitro phosphoglucosamine mutase GlmM which catalyzes the first step in the biosynthetic pathway leading to the formation of UDP-N-acetylglucosamine, an essentialcommon precursor to cell envelope components

Czech name

Charakterizace serin/threonin proteinkinázy a fosfatázy eukaryotního typu u Streptococcus pneumoniae a určení kinázových substrátů

Czech description

Byla provedena detailní biochemická studie serin/threoninové proteinkinázy StkP a proteinfosfatázy PhpP eukaryotního typu u Streptococcus pneumoniae. Analýzou fosfoproteomových map výchozího kmene a mutanta byly identifikovány dva potenciální substráty.Jeden z nich.fosfoglukosaminmutasa katalyzuje tvorbu UDP-N-acetylglukosaminu, prekurzoru složek buněčné stěny

Type

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

CEP classification

EE - Microbiology, virology

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2005

Confidentiality

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

Name of the periodical

FEBS Journal

ISSN

1742-4658

e-ISSN

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Volume of the periodical

272

Issue of the periodical within the volume

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Country of publishing house

DE - GERMANY

Number of pages

11

Pages from-to

1243-1254

UT code for WoS article

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EID of the result in the Scopus database

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