Literature summary for 2.3.1.180 extracted from

Sachdeva, S.; Musayev, F.; Alhamadsheh, M.M.; Neel Scarsdale, J.; Tonie Wright, H.; Reynolds, K.A.
Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates (2008), Bioorg. Chem., 36, 85-90.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of the mtFabH/decyl-CoA disulfide is achieved using the hanging-drop vapour-diffusion technique. The active site cysteine in both subunits of the wild type mtFabH dimer is able to react with either a dodecanoyl-CoA substrate or a decyl-CoA disulfide inhibitor	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	wild type and C122A mtFabH proteins are overexpressed in Escherichia coli with N-terminal polyhistidine tag	-

Synonyms

Synonyms	Comment	Organism
mtFabH	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)