CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.47.10
Functional Family 3-oxoacyl-[acyl-carrier-protein] synthase 2

Enzyme Information

2.3.1.41
Beta-ketoacyl-[acyl-carrier-protein] synthase I.
based on mapping to UniProt H8ESN0
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
-!- Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. -!- Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. -!- Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)). -!- The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.

UniProtKB Entries (1)

H8ESN0
FAB1_MYCTE
Mycobacterium tuberculosis str. Erdman = ATCC 35801
3-oxoacyl-[acyl-carrier-protein] synthase 1

PDB Structure

PDB 5W2S
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Synergistic Lethality of a Binary Inhibitor of Mycobacterium tuberculosis KasA.
Kumar, P., Capodagli, G.C., Awasthi, D., Shrestha, R., Maharaja, K., Sukheja, P., Li, S.G., Inoyama, D., Zimmerman, M., Ho Liang, H.P., Sarathy, J., Mina, M., Rasic, G., Russo, R., Perryman, A.L., Richmann, T., Gupta, A., Singleton, E., Verma, S., Husain, S., Soteropoulos, P., Wang, Z., Morris, R., Porter, G., Agnihotri, G., Salgame, P., Ekins, S., Rhee, K.Y., Connell, N., Dartois, V., Neiditch, M.B., Freundlich, J.S., Alland, D.
MBio