Partial Purification and Characterization of d-Ribose-5-phosphate Reductase from Adonis vernalis L. Leaves.

Abstract:

:This study presents evidence for a new enzyme, d-ribose-5-P reductase, which catalyzes the reaction: d-ribose-5-P + NADPH + H(+) --> d-ribitol-5-P + NADP(+). The enzyme was isolated from Adonis vernalis L. leaves in 38% yield and was purified 71-fold. The reductase was NADPH specific and had a pH optimum in the range of 5.5 to 6.0. The Michaelis constant value for d-ribose-5-P reduction was 1.35 millimolar. The enzyme also reduced d-erythrose-4-P, d-erythrose, dl-glyceraldehyde, and the aromatic aldehyde 3-pyridinecarboxaldehyde. Hexoses, hexose phosphates, pentoses, and dihydroxyacetone did not serve as substrates. d-Ribose-5-P reductase is distinct from the other known ribitol synthesizing enzymes detected in bacteria and yeast, and may be responsible for ribitol synthesis in Adonis vernalis.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Negm FB,Marlow GC

doi

10.1104/pp.78.4.758

subject

Has Abstract

pub_date

1985-08-01 00:00:00

pages

758-61

issue

4

eissn

0032-0889

issn

1532-2548

journal_volume

78

pub_type

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