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Literature summary for 2.3.1.301 extracted from

  • Veyron-Churlet, R.; Molle, V.; Taylor, R.; Brown, A.; Besra, G.; Zanella-Cleon, I.; Fuetterer, K.; Kremer, L.
    The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue (2009), J. Biol. Chem., 284, 6414-6424 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
T45A complete loss of activity Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WNG3
-
-
Mycobacterium tuberculosis H37Rv P9WNG3
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein FabH is efficiently phosphorylated in vitro by several mycobacterial Ser/Thr protein kinases, particularly by PknF and PknA, as well as in vivo. Residues Thr45 is the unique phosphoacceptor. Thr 45 is located at the entrance of the substrate channel Mycobacterium tuberculosis