P450(camr), a cytochrome P450 catalysing the stereospecific 6-endo-hydroxylation of (1R)-(+)-camphor

G  Grogan; G A  Roberts; S  Parsons; N J  Turner; S L  Flitsch

doi:10.1007/s00253-002-1054-0

P450(camr), a cytochrome P450 catalysing the stereospecific 6-endo-hydroxylation of (1R)-(+)-camphor

G Grogan, G A Roberts, S Parsons, N J Turner, S L Flitsch

Chemistry

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

Abstract

Rhodococcus sp. NCIMB 9784 accumulated 6-endo-hydroxycamphor 3 when grown on (1R)-(+)camphor 1 as sole carbon source. The structure of 3 has been unambiguously assigned for the first time using Xray crystallography. A soluble cytochrome P450 hydroxylase, induced by growth on (1R)-(+)-camphor and designated P450(camr), has been isolated from the bacterium Rhodococcus sp. NCIMB 9784. Using authentic 6-endo hydroxycamphor as standard, a cell-free system consisting of pure P450(camr) and putidaredoxin and putidaredoxin reductase from Pseudomonas putida confirmed that the enzyme hydroxylates (1R)-(+)-camphor specifically in the 6-endo position, in contrast to the 5-exo hydroxylation catalysed by the well-studied P450(cam) from P. putida. P450(camr) has a molecular mass of approximately 44 kDa, and a pI of 4.8.

Original language	English
Pages (from-to)	449-454
Number of pages	6
Journal	APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume	59
Issue number	4-5
DOIs	https://doi.org/10.1007/s00253-002-1054-0
Publication status	Published - Aug 2002

Keywords

RETRO-CLAISEN REACTION
CRYSTAL-STRUCTURE
BETA-DIKETONES
DESYMMETRIZATION
HYDROXYLATION
OXIDATION
CAMPHOR

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10.1007/s00253-002-1054-0

Cite this

@article{7caf0aad2b284743ab1e51e0077aaba4,

title = "P450(camr), a cytochrome P450 catalysing the stereospecific 6-endo-hydroxylation of (1R)-(+)-camphor",

abstract = "Rhodococcus sp. NCIMB 9784 accumulated 6-endo-hydroxycamphor 3 when grown on (1R)-(+)camphor 1 as sole carbon source. The structure of 3 has been unambiguously assigned for the first time using Xray crystallography. A soluble cytochrome P450 hydroxylase, induced by growth on (1R)-(+)-camphor and designated P450(camr), has been isolated from the bacterium Rhodococcus sp. NCIMB 9784. Using authentic 6-endo hydroxycamphor as standard, a cell-free system consisting of pure P450(camr) and putidaredoxin and putidaredoxin reductase from Pseudomonas putida confirmed that the enzyme hydroxylates (1R)-(+)-camphor specifically in the 6-endo position, in contrast to the 5-exo hydroxylation catalysed by the well-studied P450(cam) from P. putida. P450(camr) has a molecular mass of approximately 44 kDa, and a pI of 4.8.",

keywords = "RETRO-CLAISEN REACTION, CRYSTAL-STRUCTURE, BETA-DIKETONES, DESYMMETRIZATION, HYDROXYLATION, OXIDATION, CAMPHOR",

author = "G Grogan and Roberts, {G A} and S Parsons and Turner, {N J} and Flitsch, {S L}",

year = "2002",

month = aug,

doi = "10.1007/s00253-002-1054-0",

language = "English",

volume = "59",

pages = "449--454",

journal = "APPLIED MICROBIOLOGY AND BIOTECHNOLOGY",

issn = "0175-7598",

publisher = "Springer",

number = "4-5",

}

TY - JOUR

T1 - P450(camr), a cytochrome P450 catalysing the stereospecific 6-endo-hydroxylation of (1R)-(+)-camphor

AU - Grogan, G

AU - Roberts, G A

AU - Parsons, S

AU - Turner, N J

AU - Flitsch, S L

PY - 2002/8

Y1 - 2002/8

N2 - Rhodococcus sp. NCIMB 9784 accumulated 6-endo-hydroxycamphor 3 when grown on (1R)-(+)camphor 1 as sole carbon source. The structure of 3 has been unambiguously assigned for the first time using Xray crystallography. A soluble cytochrome P450 hydroxylase, induced by growth on (1R)-(+)-camphor and designated P450(camr), has been isolated from the bacterium Rhodococcus sp. NCIMB 9784. Using authentic 6-endo hydroxycamphor as standard, a cell-free system consisting of pure P450(camr) and putidaredoxin and putidaredoxin reductase from Pseudomonas putida confirmed that the enzyme hydroxylates (1R)-(+)-camphor specifically in the 6-endo position, in contrast to the 5-exo hydroxylation catalysed by the well-studied P450(cam) from P. putida. P450(camr) has a molecular mass of approximately 44 kDa, and a pI of 4.8.

AB - Rhodococcus sp. NCIMB 9784 accumulated 6-endo-hydroxycamphor 3 when grown on (1R)-(+)camphor 1 as sole carbon source. The structure of 3 has been unambiguously assigned for the first time using Xray crystallography. A soluble cytochrome P450 hydroxylase, induced by growth on (1R)-(+)-camphor and designated P450(camr), has been isolated from the bacterium Rhodococcus sp. NCIMB 9784. Using authentic 6-endo hydroxycamphor as standard, a cell-free system consisting of pure P450(camr) and putidaredoxin and putidaredoxin reductase from Pseudomonas putida confirmed that the enzyme hydroxylates (1R)-(+)-camphor specifically in the 6-endo position, in contrast to the 5-exo hydroxylation catalysed by the well-studied P450(cam) from P. putida. P450(camr) has a molecular mass of approximately 44 kDa, and a pI of 4.8.

KW - RETRO-CLAISEN REACTION

KW - CRYSTAL-STRUCTURE

KW - BETA-DIKETONES

KW - DESYMMETRIZATION

KW - HYDROXYLATION

KW - OXIDATION

KW - CAMPHOR

U2 - 10.1007/s00253-002-1054-0

DO - 10.1007/s00253-002-1054-0

M3 - Article

SN - 0175-7598

VL - 59

SP - 449

EP - 454

JO - APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

JF - APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

IS - 4-5

ER -