Cloning and sequencing of cDNA encoding 4-aminobenzoate hydroxylase fromAgaricus bisporus
Author:
Publisher
Elsevier BV
Subject
Genetics,Biochemistry,Biophysics,Structural Biology
Reference24 articles.
1. A unique enzyme catalyzing the formation of 4-hydroxyaniline from 4-aminobenzoic acid in Agaricus bisporus
2. Purification and properties of 4-aminobenzoate hydroxylase, a new monooxygenase from Agaricus bisporus.
3. Incorporation of radioactive shikimic acid into N-(γ-Lglutamyl)-4-hydroxyaniline in Agaricus bisporus
4. Incorporation of chorismic acid and 4-aminobenzoic acid into the 4-hydroxyaniline moiety of N-(γ-L-glutamyl)-4-hydroxyaniline in Agaricusbisporus
5. The influence of purification and protein heterogeneity on the crystallization of p-hydroxybenzoate hydroxylase
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1. Identification and characterization of a pab gene cluster responsible for the 4-aminobenzoate degradation pathway, including its involvement in the formation of a γ-glutamylated intermediate in Paraburkholderia terrae strain KU-15;Journal of Bioscience and Bioengineering;2024-01
2. A 4-hydroxybenzoate 3-hydroxylase mutant enables 4-amino-3-hydroxybenzoic acid production from glucose in Corynebacterium glutamicum;2023-06-09
3. Quantitative proteomic analysis of the microbial degradation of 3-aminobenzoic acid by Comamonas sp. QT12;Scientific Reports;2022-10-20
4. A novel gene, encoding 3-aminobenzoate 6-monooxygenase, involved in 3-aminobenzoate degradation in Comamonas sp. strain QT12;Applied Microbiology and Biotechnology;2018-04-25
5. A Single-Site Mutation at Ser146 Expands the Reactivity of the Oxygenase Component of p-Hydroxyphenylacetate 3-Hydroxylase;ACS Chemical Biology;2016-09-06
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