Phosphorylation of protein kinase Cdelta (PKCdelta) at threonine 505 is not a prerequisite for enzymatic activity. Expression of rat PKCdelta and an alanine 505 mutant in bacteria in a functional form.

doi:10.1074/jbc.272.10.6805

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Article

Phosphorylation of protein kinase Cdelta (PKCdelta) at threonine 505 is not a prerequisite for enzymatic activity. Expression of rat PKCdelta and an alanine 505 mutant in bacteria in a functional form.

The Journal of biological chemistry - 7 Mar 1997

Stempka L, Girod A, Müller H J, Rincke G, Marks F, Gschwendt M, Bossemeyer D

Abstract excerpt

A structural feature shared by many protein kinases is the requirement for phosphorylation of threonine or tyrosine in the so-called activation loop for full enzyme activity. Previous studies by several groups have indicated that the isotypes alpha, betaI, and betaII of protein kinase C (PKC) are...

Topics

Alanine
Animals
Baculoviridae
Enzyme Inhibitors
Escherichia coli
Isoenzymes
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Phosphorylation
Protein Kinase C

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Kinase C-delta

Protein Structure, Tertiary

Rats

Recombinant Proteins

Spodoptera

Structure-Activity Relationship

Threonine

Source

Open in PubMed

Identifiers

PMID: 9045715
DOI: 10.1074/jbc.272.10.6805

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9045715-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Phosphorylation of protein kinase Cdelta (PKCdelta) at threonine 505 is not a prerequisite for enzymatic activity. Expression of rat PKCdelta and an alanine 505 mutant in bacteria in a functional form.PMID 9045715Read ↗

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