☆ 4.6 Article

Hidden Function of Catalytic Domain in 6-Methylsalicylic Acid Synthase for Product Release

JOURNAL OF BIOLOGICAL CHEMISTRY (2010)

Journal

JOURNAL OF BIOLOGICAL CHEMISTRY

Volume 285, Issue 20, Pages 15637-15643

Publisher

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

DOI: 10.1074/jbc.M110.107391

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Categories

Biochemistry & Molecular Biology

Funding

Japan Society for the Promotion of Science [19310139]
Ministry of Education, Culture, Sports, Science, and Technology of Japan
Grants-in-Aid for Scientific Research [19310139] Funding Source: KAKEN

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Abstract

Functional investigation of the proposed dehydratase domain of ATX, a 6-methylsalicylic acid synthase from Aspergillus terreus, revealed that the domain is not involved in dehydration of the beta-hydroxytriketide intermediate tethered on the acyl carrier protein but catalyzes thioester hydrolysis to release the product from the acyl carrier protein. Thus, we renamed this domain the thioester hydrolase (TH) domain. The intermediate bound to the TH domain of mutant H972A formed in the presence of NADPH was released as 6-methylsalicylic acid by both the intact ATX and by THID (a 541-amino acid region containing TH domain and its downstream) protein, in trans. Furthermore, THID showed a catalytic activity to hydrolyze a model substrate, 6-methylsalicylic acid-N-acetylcysteamine. The TH domain is the first example of a product-releasing domain that is located in the middle of a multidomain iterative type I polyketide synthase. Moreover, it is functionally different from serine protease-type thioesterase domains of iterative type I polyketide synthases.

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