Biohydroxylation reactions catalyzed by enzymes and whole-cell systems

S L  Flitsch; S J  Aitken; C S Y  Chow; G  Grogan; A  Staines

Biohydroxylation reactions catalyzed by enzymes and whole-cell systems

S L Flitsch, S J Aitken, C S Y Chow, G Grogan, A Staines

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

The biohydroxylation of a number of cyclic substrates (3-24) containing aromatic side chains was used to compare substrate specificity and selectivity of hydroxylation using microbial enzymes and whole-cell biocatalysts. In general, the regioselectivity of reaction was remarkably similar between the different catalysts in that little aromatic or benzylic, but significant aliphatic hydroxylation was observed. However, a more detailed investigation of isolated products showed complementary substrate specificity, functional group compatibility, and regioselectivity of hydroxylation. Substrate specificity and regioselectivity could be further modulated by small changes to the nature of the aromatic side chain, which appears to play an important role in substrate recognition, (C) 1999 Academic Press.

Original language	English
Pages (from-to)	81-90
Number of pages	10
Journal	RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
Volume	27
Issue number	2
Publication status	Published - Apr 1999

Keywords

CYTOCHROME P450(CAM)
PSEUDOMONAS-PUTIDA
ESCHERICHIA-COLI
HYDROXYLATION
MONOOXYGENASE
NAPHTHALENE
OXIDATION

Cite this

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title = "Biohydroxylation reactions catalyzed by enzymes and whole-cell systems",

abstract = "The biohydroxylation of a number of cyclic substrates (3-24) containing aromatic side chains was used to compare substrate specificity and selectivity of hydroxylation using microbial enzymes and whole-cell biocatalysts. In general, the regioselectivity of reaction was remarkably similar between the different catalysts in that little aromatic or benzylic, but significant aliphatic hydroxylation was observed. However, a more detailed investigation of isolated products showed complementary substrate specificity, functional group compatibility, and regioselectivity of hydroxylation. Substrate specificity and regioselectivity could be further modulated by small changes to the nature of the aromatic side chain, which appears to play an important role in substrate recognition, (C) 1999 Academic Press.",

keywords = "CYTOCHROME P450(CAM), PSEUDOMONAS-PUTIDA, ESCHERICHIA-COLI, HYDROXYLATION, MONOOXYGENASE, NAPHTHALENE, OXIDATION",

author = "Flitsch, {S L} and Aitken, {S J} and Chow, {C S Y} and G Grogan and A Staines",

year = "1999",

month = apr,

language = "English",

volume = "27",

pages = "81--90",

journal = "RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY",

issn = "1068-1620",

publisher = "Academic Press",

number = "2",

}

TY - JOUR

T1 - Biohydroxylation reactions catalyzed by enzymes and whole-cell systems

AU - Flitsch, S L

AU - Aitken, S J

AU - Chow, C S Y

AU - Grogan, G

AU - Staines, A

PY - 1999/4

Y1 - 1999/4

N2 - The biohydroxylation of a number of cyclic substrates (3-24) containing aromatic side chains was used to compare substrate specificity and selectivity of hydroxylation using microbial enzymes and whole-cell biocatalysts. In general, the regioselectivity of reaction was remarkably similar between the different catalysts in that little aromatic or benzylic, but significant aliphatic hydroxylation was observed. However, a more detailed investigation of isolated products showed complementary substrate specificity, functional group compatibility, and regioselectivity of hydroxylation. Substrate specificity and regioselectivity could be further modulated by small changes to the nature of the aromatic side chain, which appears to play an important role in substrate recognition, (C) 1999 Academic Press.

AB - The biohydroxylation of a number of cyclic substrates (3-24) containing aromatic side chains was used to compare substrate specificity and selectivity of hydroxylation using microbial enzymes and whole-cell biocatalysts. In general, the regioselectivity of reaction was remarkably similar between the different catalysts in that little aromatic or benzylic, but significant aliphatic hydroxylation was observed. However, a more detailed investigation of isolated products showed complementary substrate specificity, functional group compatibility, and regioselectivity of hydroxylation. Substrate specificity and regioselectivity could be further modulated by small changes to the nature of the aromatic side chain, which appears to play an important role in substrate recognition, (C) 1999 Academic Press.

KW - CYTOCHROME P450(CAM)

KW - PSEUDOMONAS-PUTIDA

KW - ESCHERICHIA-COLI

KW - HYDROXYLATION

KW - MONOOXYGENASE

KW - NAPHTHALENE

KW - OXIDATION

M3 - Article

SN - 1068-1620

VL - 27

SP - 81

EP - 90

JO - RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY

JF - RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY

IS - 2

ER -