Nicotinamide Adenine Dinucleotide-dependent Proline Dehydrogenase in Chlorella.

Plant physiology ·Vol. 53 ·No. 3 ·1974-03-00 ·Pages 440-4

McNamer AD, Stewart CR

Abstract

An NAD-linked dehydrogenase from Chlorella pyrenoidosa Chick catalyzing the conversion of l-proline to Delta(1)-pyrroline-5-carboxylic acid was partially purified. Delta(1)-Pyrroline-5-carboxylic acid was identified as the product by co-chromatography of it and its o-aminobenzaldehyde derivative with authentic compounds. The enzyme is NAD and l-proline specific and is not an oxidase; NADP is not inhibitory. The Michaelis constant for NAD is 0.08 mm and for proline is 0.73 mm.

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

McNamer A D

Department of Botany and Plant Pathology, Iowa State University, Ames, Iowa 50010.

Stewart C R

References (11)

11 references, click to expand

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Article Info

Journal

Plant physiology

Abbr.

Plant Physiol

ISSN

0032-0889

DOI

10.1104/pp.53.3.440

Published

1974-03-00

Pages

440-4

Language

English

Region

United States

NLM ID

0401224

PMCID

PMC543244

External Links

PubMed source DOI: 10.1104/pp.53.3.440 PMC Full Text View journal details

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Nicotinamide Adenine Dinucleotide-dependent Proline Dehydrogenase in Chlorella.

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