Comparative studies on substrate specificity of succinic semialdehyde reductase from <i>Gluconobacter oxydans</i> and glyoxylate reductase from <i>Acetobacter aceti</i>-Reference-Cited by-同舟云学术

Comparative studies on substrate specificity of succinic semialdehyde reductase from Gluconobacter oxydans and glyoxylate reductase from Acetobacter aceti

Published:2024-06-13 Issue:9 Volume:88 Page:1069-1072
ISSN:1347-6947
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Majumder Toma Rani¹,Inoue Masao¹²,Aono Riku¹,Ochi Anna¹,Mihara Hisaaki¹^ORCID

Affiliation:

1. College of Life Sciences, Ritsumeikan University , Kusatsu, Shiga , Japan

2. R-GIRO, Ritsumeikan University , Kusatsu, Shiga , Japan

Abstract

Abstract Gluconobacter oxydans succinic semialdehyde reductase (GoxSSAR) and Acetobacter aceti glyoxylate reductase (AacGR) represent a novel class in the β-hydroxyacid dehydrogenases superfamily. Kinetic analyses revealed GoxSSAR's activity with both glyoxylate and succinic semialdehyde, while AacGR is glyoxylate specific. GoxSSAR K167A lost activity with succinic semialdehyde but retained some with glyoxylate, whereas AacGR K175A lost activity. These findings elucidate differences between these homologous enzymes.

Funder

Ritsumeikan Global Innovation Research Organization, Ritsumeikan University

Publisher

Oxford University Press (OUP)

Link

https://academic.oup.com/bbb/advance-article-pdf/doi/10.1093/bbb/zbae081/58470572/zbae081.pdf

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