Literature summary for 2.3.1.122 extracted from

Warrier, T.; Tropis, M.; Werngren, J.; Diehl, A.; Gengenbacher, M.; Schlegel, B.; Schade, M.; Oschkinat, H.; Daffe, M.; Hoffner, S.; Eddine, A.N.; Kaufmann, S.H.
Antigen 85C inhibition restricts Mycobacterium tuberculosis growth through disruption of cord factor biosynthesis (2012), Antimicrob. Agents Chemother., 56, 1735-1743.

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Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression as C-terminally His-tagged enzyme	Mycobacterium tuberculosis

Inhibitors

Inhibitors	Comment	Organism	Structure
2-amino-6-propyl-4,5,6,7-tetrahydro-1-benzothiophene-3-carbonitrile	i.e. I3-AG85, enzyme inhibition leads to accumulation of trehalose monomycolate and disruption of the bacterial envelope, I3-AG85 also inhibits Mycobacterium tuberculosis survival in infected primary macrophages. Binding of I3-AG85 to Ag85C is similar to its binding to the artificial substrate octylthioglucoside, overview	Mycobacterium tuberculosis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WQN9	and clinical isolates MT103 and MYC1554, dru-resistant Ag85C mutants	-
Mycobacterium tuberculosis H37Rv	P9WQN9	and clinical isolates MT103 and MYC1554, dru-resistant Ag85C mutants	-

Synonyms

Synonyms	Comment	Organism
ag85C	-	Mycobacterium tuberculosis
mycoloyl transferase	-	Mycobacterium tuberculosis

General Information

General Information	Comment	Organism
malfunction	inhibition of Ag85 protein family enzymes through substrate analogs hinders growth of mycobacteria and inhibition of Ag85C leads to accumulation of trehalose monomycolate	Mycobacterium tuberculosis
physiological function	the mycoloyl transferase activity of antigen 85 (Ag85) protein family, consisting of Ag85A, -B, and -C, generates trehalose dimycolate, an envelope lipid essential for Mycobacterium tuberculosis virulence, and cell wall arabinogalactan-linked mycolic acids	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)