Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2-Reference-Cited by-同舟云学术

Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2

Published:1996-11 Issue:22 Volume:178 Page:6623-6627
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

French C E¹,Nicklin S¹,Bruce N C¹

Affiliation:

1. Institute of Biotechnology, University of Cambridge, United Kingdom.

Abstract

Pentaerythritol tetranitrate reductase, which reductively liberates nitrite from nitrate esters, is related to old yellow enzyme. Pentaerythritol tetranitrate reductase follows a ping-pong mechanism with competitive substrate inhibition by NADPH, is strongly inhibited by steroids, and is capable of reducing the unsaturated bond of 2-cyclohexen-1-one.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jb.178.22.6623-6627.1996

Reference21 articles.

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2. Cleland W. W. 1970. Steady state enzyme kinetics p. 1-65. In P. D. Boyer (ed.) The enzymes 3rd ed. vol. 2. Academic Press Inc. N.Y.

3. Old yellow enzyme at 2 Å resolution: overall structure, ligand binding, and comparison with related flavoproteins;Fox K. M.;Structure,1994

4. Purification and characterization of morphinone reductase from Pseudomonas putida M10;French C. E.;Biochem. J.,1994

5. Bacterial morphinone reductase is related to old yellow enzyme;French C. E.;Biochem. J.,1995

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