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Literature summary extracted from

  • Sachdeva, S.; Musayev, F.N.; Alhamadsheh, M.M.; Scarsdale, J.N.; Wright, H.T.; Reynolds, K.A.
    Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH (2008), Chem. Biol., 15, 402-412.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.180 hanging-drop vapor diffusion method, crystal structures of mtFabH and C112A mtFabH with 1 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.180 Mycobacterium tuberculosis P9WNG3
-
-
2.3.1.180 Mycobacterium tuberculosis H37Rv P9WNG3
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 data support a new model for catalysis, in which FabH exists in an open form that permits binding of the long chain acyl-coenzyme A substrate binding and release of the corresponding 3-ketoacyl ACP product. Catalysis and intermediate steps in the process are proposed to occur in a closed form of the mtFabH. These conformational changes may be critical for binding and dissociation steps in other enzymes of the FAS pathways, including transfers between the type I and type II FASII components of Mycobacterium tuberculosis Mycobacterium tuberculosis
a

Synonyms

EC Number Synonyms Comment Organism
2.3.1.180 FabH
-
 Mycobacterium tuberculosis