| EC |
2.3.1.165 |
| Accepted name: |
6-methylsalicylic-acid synthase |
| Reaction: |
acetyl-CoA + 3 malonyl-CoA + NADPH + H+ = 6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O |
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For diagram of polyketides biosynthesis, click here |
| Other name(s): |
MSAS; 6-methylsalicylic acid synthase |
| Systematic name: |
acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl-reducing, thioester-hydrolysing and cyclizing) |
| Comments: |
A multienzyme complex with a tightly-bound 4′-phosphopantetheine cofactor on the acyl carrier protein. It has a similar sequence to vertebrate type I fatty acid synthase. Acetoacetyl-CoA can also act as a starter molecule. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9045-37-8 |
| References: |
| 1. |
Spencer, J.B. and Jordan, P.M. Purification and properties of 6-methylsalicylic acid synthase from Penicillium patulum. Biochem. J. 288 (1992) 839–846. [PMID: 1471999] |
| 2. |
Child, C.J., Spencer, J.B., Bhogal, P. and Shoolingin-Jordan, P.M. Structural similarities between 6-methylsalicylic acid synthase from Penicillium patulum and vertebrate type I fatty acid synthase: evidence from thiol modification studies. Biochemistry 35 (1996) 12267–12274. [DOI] [PMID: 8823160] |
| 3. |
Richardson, M.T., Pohl, N.L., Kealey, J.T. and Khosla, C. Tolerance and specificity of recombinant 6-methylsalicyclic acid synthase. Metab. Eng. 1 (1999) 180–187. [DOI] [PMID: 10935930] |
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| [EC 2.3.1.165 created 2002] |
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