Abstract |
In Mycobacterium tuberculosis, signal transduction is mediated by 11 serine/threonine kinases, but no tyrosine kinases have been identified thus far. The protein encoded by the ORF (open reading frame) Rv2232 has been annotated as a member of the HAD (haloacid dehydrogenase-like hydrolase) superfamily, which includes phosphatases, phosphomanno- and phosphogluco-mutases, and haloacid dehydrogenases. In the present paper, we report, on the basis of biochemical and mutational analyses, that the Rv2232-encoded protein, named protein tyrosine kinase A (PtkA) is a bona fide protein tyrosine kinase. The cognate substrate of PtkA is the secreted protein tyrosine phosphatase A (PtpA).
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Authors | Horacio Bach, Dennis Wong, Yossef Av-Gay |
Journal | The Biochemical journal
(Biochem J)
Vol. 420
Issue 2
Pg. 155-60
(May 13 2009)
ISSN: 1470-8728 [Electronic] England |
PMID | 19366344
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Bacterial Proteins
- Tyrosine
- Protein-Tyrosine Kinases
- Receptor-Like Protein Tyrosine Phosphatases, Class 4
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Topics |
- Amino Acid Substitution
- Bacterial Proteins
(genetics, metabolism)
- Binding, Competitive
- Kinetics
- Mutation
- Mycobacterium tuberculosis
(enzymology, genetics, metabolism)
- Phosphorylation
- Protein Binding
- Protein-Tyrosine Kinases
(genetics, metabolism)
- Receptor-Like Protein Tyrosine Phosphatases, Class 4
(genetics, metabolism)
- Substrate Specificity
- Tyrosine
(metabolism)
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