Structure, dimeric conformation, and coenzyme versatility of p-hydroxybenzoate hydroxylase from Arthrobacter sp. PAMC25564-Reference-Cited by-同舟云学术

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Structure, dimeric conformation, and coenzyme versatility of p-hydroxybenzoate hydroxylase from Arthrobacter sp. PAMC25564

Published:2024-08 Issue: Volume:274 Page:133268
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Ghimire Nisha,Kim Subin,Park Hyun Ho,Oh Tae-Jin

Publisher

Elsevier BV

Reference41 articles.

1. Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts;Van Berkel;J. Biotechnol.,2006

2. Flavin dependent monooxygenases;Huijbers;Arch. Biochem. Biophys.,2014

3. Flavoprotein monooxygenases: versatile biocatalysts;Paul;Biotechnol. Adv.,2021

4. A study of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens: improved purification, relative molecular mass, and amino acid composition;Müller;Eur. J. Biochem.,1979

5. Crystal structure of p-hydroxybenzoate hydroxylase;Wierenga;J. Mol. Biol.,1979

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