Indole-3-Ethanol Oxidase in Phycomyces blakesleeanus Bgff | Zendy

Peter Schramm | Zendy; Thomas Rausch | Zendy; Willy Hilgenberg | Zendy

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Indole-3-Ethanol Oxidase in Phycomyces blakesleeanus Bgff

Author(s) -

Peter Schramm,

Thomas Rausch,

Willy Hilgenberg

Publication year - 1987

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.84.2.541

Subject(s) - chemistry , phycomyces blakesleeanus , indole test , enzyme , acetaldehyde , oxidase test , flavin group , ammonium sulfate , ethanol , flavin adenine dinucleotide , biochemistry , phycomyces , enzyme assay , stereochemistry , chromatography , cofactor , mutant , gene

Indole-3-ethanol oxidase (IEt oxidase) from Phycomyces blakesleeanus Bgff.(P.b.) is a 56 kD polypeptide as determined by gel filtration. The reaction products are indole-3-acetaldehyde (IAAld) and, possibly, H(2)O(2). Enzyme activity (33-45% ammonium sulfate fraction) shows a broad pH optimum and simple Michaelis-Menten kinetics (K(m) 7 micromolar, Hill coefficient 0.95). Flavin adenine dinucleotide increases enzyme activity particularly under anaerobic conditions. Iodoacetate and HgCl(2) drastically inhibit the enzyme. With IAAld, product inhibition is observed at micromolar concentrations. IAA and some other acidic substituted indoles reduce enzyme activity but only at higher concentrations.

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