当前位置： SCI文献检索 > ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS期刊下所有文献 > Identification, characterization, and partial purification of 4 alpha-carboxysterol-C3-dehydrogenase/ C4-decarboxylase from Zea mays.

Identification, characterization, and partial purification of 4 alpha-carboxysterol-C3-dehydrogenase/ C4-decarboxylase from Zea mays.

Abstract：

:A microsomal preparation from seedlings of Zea mays catalyzed the NAD+-dependent oxidative decarboxylation of several substrates, including 4alpha-carboxy-cholest-7-en-3beta-ol, synthesized according to a new procedure, giving the first in vitro evidence for this enzymatic activity in a higher plant. A GC assay has been developed to detect the Delta7-cholestenone produced and the kinetic parameters of the microsomal system have been established. 4alpha-Carboxysterol decarboxylation shows an exclusive requirement for an oxidized pyridine nucleotide, with NAD+ being more efficient than NADP+. The decarboxylation reaction is independent of molecular oxygen. 4alpha-Carboxysterol-C3-dehydrogenase/C4-decarboxylase (4alpha-CD) is a microsome-bound protein which can be efficiently solubilized by detergents, including Brij W-1 and sodium cholate. The Brij W-1-solubilized enzyme was partially purified 290-fold by a combination of DEAE anion-exchange chromatography, Cibacron blue 3GA-agarose dye chromatography, and gel permeation. The apparent molecular mass of 4alpha-CD in sodium cholate was estimated to be 45 kDa. These results support the contention that demethylation at C4 of plant sterols is composed of two separate processes: an oxygen- and NAD(P)H-dependent oxidation of the 4alpha-methyl group to produce the 4alpha-carboxysterol metabolite (S. Pascal et al., J. Biol. Chem. 268, 11639, 1993) followed by oxygen-independent dehydrogenation/decarboxylation to produce an obligatory 3-ketosteroid.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Rondet S,Taton M,Rahier A

doi

10.1006/abbi.1999.1218

subject

Has Abstract

pub_date

1999-06-15 00:00:00

pages

249-60

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(99)91218-3

journal_volume

366

pub_type

杂志文章

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