Unusual arrangement of catalytic domains in head-to-tail associated homodimer of 6-hydroxymellein synthase, a multifunctional polyketide biosynthetic enzyme
Author:
Publisher
Elsevier BV
Subject
Plant Science,Agronomy and Crop Science,Genetics,General Medicine
Reference19 articles.
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3. Dimer as the active form of a polyketide biosynthetic enzyme 6- hydroxymellein synthase;Kurosaki;Phytochemistry,1995
4. Dissociation of dimeric 6-hydroxymellein synthase, a polyketide biosynthetic enzyme in carrot cell extracts, with loss of ketoreducing activity;Kurosaki;Arch. Biochem. Biophys.,1995
5. Structure and mechanism of fatty acid synthetase;Wakil,1983
Cited by 1 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Regulation of catalytic activity of a multifunctional polyketide biosynthetic enzyme, 6-hydroxymellein synthase, by interaction between NADPH and phenylglyoxal-sensitive amino acid residue at the reaction center;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2001-09
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