Isolation of a multi-enzyme complex of fatty acid oxidation from Escherichia coli. | Zendy

Judith Feigenbaum Binstock | Zendy; A Pramanik | Zendy; Horst Schulz | Zendy

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Isolation of a multi-enzyme complex of fatty acid oxidation from Escherichia coli.

Author(s) -

Judith Feigenbaum Binstock,

A Pramanik,

Horst Schulz

Publication year - 1977

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.74.2.492

Subject(s) - thiolase , escherichia coli , enzyme , biochemistry , beta oxidation , chemistry , dehydrogenase , fatty acid , molecular mass , long chain fatty acid , biology , gene

A multi-enzyme complex of fatty acid oxidation has been isolated from E. coli B cells and has been purified to near homogeneity by a simple two-step procedure. The complex exhibits thiolase (EC 2.3.1.9), enoyl-CoA hydratase (EC 4.2.1.17), and 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) activities towards short-, medium-, and long-chain substrates. The complex has been estimated to have a molecular weight of approximately 300,000 and is apparently composed of two types of subunits with molecular weights of 78,000 and 42,000.

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