7α-Dehydroxylation of cholic acid by cell extracts of Eubacterium species V.P.I. 12708

P. B. Hylemon; A. F. Cacciapuoti; B. A. White; T. R. Whitehead; R. J. Fricke

doi:10.1093/ajcn/33.11.2507

7α-Dehydroxylation of cholic acid by cell extracts of Eubacterium species V.P.I. 12708

P. B. Hylemon
, A. F. Cacciapuoti
, B. A. White
, T. R. Whitehead
, R. J. Fricke

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

Abstract

NADH:flavin oxidoreductase and 7α-dehydroxylase were induced 5- and 90-fold, respectively, by cholic acid in cultures of Eubacterium species V.P.I. 12708. Assays of 7α-dehydroxylase activity in the presence of various cofactors revealed that optimal activity was obtained in the presence of NAD⁺ plus FADH₂. The pH optima of 7α-dehydroxylase activity in whole cells and cell extracts were 7.0. The similar induction pattern of these two enzymes and the apparent cofactor requirements for 7α-dehydroxylation suggest a relationship between 7α-dehydroxylase and NADH:flavin oxidoreductase.

Original language	English (US)
Pages (from-to)	2507-2510
Number of pages	4
Journal	American Journal of Clinical Nutrition
Volume	33
Issue number	11 SUPPL.
DOIs	https://doi.org/10.1093/ajcn/33.11.2507
State	Published - 1980
Externally published	Yes

ASJC Scopus subject areas

Medicine (miscellaneous)
Nutrition and Dietetics

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10.1093/ajcn/33.11.2507

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title = "7α-Dehydroxylation of cholic acid by cell extracts of Eubacterium species V.P.I. 12708",

abstract = "NADH:flavin oxidoreductase and 7α-dehydroxylase were induced 5- and 90-fold, respectively, by cholic acid in cultures of Eubacterium species V.P.I. 12708. Assays of 7α-dehydroxylase activity in the presence of various cofactors revealed that optimal activity was obtained in the presence of NAD+ plus FADH2. The pH optima of 7α-dehydroxylase activity in whole cells and cell extracts were 7.0. The similar induction pattern of these two enzymes and the apparent cofactor requirements for 7α-dehydroxylation suggest a relationship between 7α-dehydroxylase and NADH:flavin oxidoreductase.",

author = "Hylemon, \{P. B.\} and Cacciapuoti, \{A. F.\} and White, \{B. A.\} and Whitehead, \{T. R.\} and Fricke, \{R. J.\}",

year = "1980",

doi = "10.1093/ajcn/33.11.2507",

language = "English (US)",

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pages = "2507--2510",

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issn = "0002-9165",

publisher = "Elsevier B.V.",

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TY - JOUR

T1 - 7α-Dehydroxylation of cholic acid by cell extracts of Eubacterium species V.P.I. 12708

AU - Hylemon, P. B.

AU - Cacciapuoti, A. F.

AU - White, B. A.

AU - Whitehead, T. R.

AU - Fricke, R. J.

PY - 1980

Y1 - 1980

N2 - NADH:flavin oxidoreductase and 7α-dehydroxylase were induced 5- and 90-fold, respectively, by cholic acid in cultures of Eubacterium species V.P.I. 12708. Assays of 7α-dehydroxylase activity in the presence of various cofactors revealed that optimal activity was obtained in the presence of NAD+ plus FADH2. The pH optima of 7α-dehydroxylase activity in whole cells and cell extracts were 7.0. The similar induction pattern of these two enzymes and the apparent cofactor requirements for 7α-dehydroxylation suggest a relationship between 7α-dehydroxylase and NADH:flavin oxidoreductase.

AB - NADH:flavin oxidoreductase and 7α-dehydroxylase were induced 5- and 90-fold, respectively, by cholic acid in cultures of Eubacterium species V.P.I. 12708. Assays of 7α-dehydroxylase activity in the presence of various cofactors revealed that optimal activity was obtained in the presence of NAD+ plus FADH2. The pH optima of 7α-dehydroxylase activity in whole cells and cell extracts were 7.0. The similar induction pattern of these two enzymes and the apparent cofactor requirements for 7α-dehydroxylation suggest a relationship between 7α-dehydroxylase and NADH:flavin oxidoreductase.

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M3 - Article

C2 - 7435421

AN - SCOPUS:0019163123

SN - 0002-9165

VL - 33

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JO - American Journal of Clinical Nutrition

JF - American Journal of Clinical Nutrition

IS - 11 SUPPL.

ER -

7α-Dehydroxylation of cholic acid by cell extracts of Eubacterium species V.P.I. 12708

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