ArticlePlant physiology1993
3-Ketoacyl-acyl carrier protein synthase III from spinach (Spinacia oleracea) is not similar to other condensing enzymes of fatty acid synthase.
Article in Plant physiology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Synthesis of CInternational journal of molecular sciences · 2022Review
- β-Ketoacyl-acyl Carrier Protein Synthase I (KASI) Plays Crucial Roles in the Plant Growth and Fatty Acids Synthesis in Tobacco.International journal of molecular sciences · 2016Article
- Article
- Cloning and sequence analysis of putative type II fatty acid synthase genes from Arachis hypogaea L.Journal of biosciences · 2009Article
- Overexpression of 3-ketoacyl-acyl-carrier protein synthase IIIs in plants reduces the rate of lipid synthesis.Plant physiology · 2001Article
- Identification of amino acid residues important in the cyclization reactions of chalcone and stilbene synthases.The Biochemical journal · 2000Article
- Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme.The Biochemical journal · 2000Article
- Article
- Identification of a chloroplast coenzyme A-binding protein related to the peroxisomal thiolases.Plant physiology · 1996Article
- New members of the barley Kas gene family encoding beta-ketoacyl-acyl carrier protein synthases.Plant physiology · 1994Article
- Cloning of a cDNA encoding 3-ketoacyl-acyl carrier protein synthase III from Arabidopsis.Plant physiology · 1994Article
- Isolation and sequence analysis of polyketide synthase genes from the daunomycin-producing Streptomyces sp. strain C5.Journal of bacteriology · 1994Article
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2 authors.
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Abstract
A cDNA clone encoding spinach (Spinacia oleracea) 3-ketoacyl-acyl carrier protein synthase III (KAS III), which catalyzes the initial condensing reaction in fatty acid biosynthesis, was isolated. Based on the amino acid sequence of tryptic digests of purified spinach KAS III, degenerate polymerase chain reaction (PCR) primers were designed and used to amplify a 612-bp fragment from first-strand cDNA of spinach leaf RNA. A root cDNA library was probed with the PCR fragment, and a 1920-bp clone was isolated. Its deduced amino acid sequence matched the sequences of the tryptic digests obtained from the purified KAS III. Northern analysis confirmed that it was expressed in both leaf and root. The clone contained a 1218-bp open reading frame coding for 405 amino acids. The identity of the clone was confirmed by expression in Escherichia coli BL 21 as a glutathione S-transferase fusion protein. The deduced amino acid sequence was 48 and 45% identical with the putative KAS III of Porphyra umbilicalis and KAS III of E. coli, respectively. It also had a strong local homology to the plant chalcone synthases but had little homology with other KAS isoforms from plants, bacteria, or animals.
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