Trapping of a novel coenzyme a containing intermediate of 3-hydroxy-3-methylglutaryl-CoA synthase

Henry M. Miziorko; David Shortle; M. Daniel Lane

doi:10.1016/S0006-291X(76)80277-X

Trapping of a novel coenzyme a containing intermediate of 3-hydroxy-3-methylglutaryl-CoA synthase

Henry M. Miziorko, David Shortle, M. Daniel Lane

School of Medicine

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

5 Scopus citations

Abstract

By controlling conditions which affect the relative rates of the partial reactions in HMG-CoA synthesis, it has been possible to trap and partially characterize HMG (-SCoA)-S-enzyme, the postulated central intermediate in catalysis. At -25° in 25% ethanol, the breakdown of HMG (-SCoA)-S-enzyme to HMG-SCoA and HS-enzyme is slowed relative to its rate of formation from acetoacetyl-SCoA and acetyl-S-enzyme. Under these conditions label from acetoacetyl-S[³H]CoA or [¹⁴C]acetyl-S-enzyme can be trapped in the accumulated intermediate with [¹⁴C] activity appearing in the HMG moiety.

Original language	English (US)
Pages (from-to)	92-98
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	69
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(76)80277-X
State	Published - Mar 8 1976

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/S0006-291X(76)80277-X

Cite this

@article{d66ed4b1fe924a6d9e14570df333f367,

title = "Trapping of a novel coenzyme a containing intermediate of 3-hydroxy-3-methylglutaryl-CoA synthase",

abstract = "By controlling conditions which affect the relative rates of the partial reactions in HMG-CoA synthesis, it has been possible to trap and partially characterize HMG (-SCoA)-S-enzyme, the postulated central intermediate in catalysis. At -25° in 25% ethanol, the breakdown of HMG (-SCoA)-S-enzyme to HMG-SCoA and HS-enzyme is slowed relative to its rate of formation from acetoacetyl-SCoA and acetyl-S-enzyme. Under these conditions label from acetoacetyl-S[3H]CoA or [14C]acetyl-S-enzyme can be trapped in the accumulated intermediate with [14C] activity appearing in the HMG moiety.",

author = "Miziorko, {Henry M.} and David Shortle and Lane, {M. Daniel}",

note = "Funding Information: ACKNOWLEDGEMENTS: This investigation was supported by grants from the National Institutes of Health, USPHS (AM-14574 and -14575) and the American Heart Association, Inc. (#73,840). H.M.M. was supported by a Postdoctoral Fellowshi~ from the National Institutes of Health, and D.S. by the Insurance Medical Scientist Scholarship Fund.",

year = "1976",

month = mar,

day = "8",

doi = "10.1016/S0006-291X(76)80277-X",

language = "English (US)",

volume = "69",

pages = "92--98",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - Trapping of a novel coenzyme a containing intermediate of 3-hydroxy-3-methylglutaryl-CoA synthase

AU - Miziorko, Henry M.

AU - Shortle, David

AU - Lane, M. Daniel

N1 - Funding Information: ACKNOWLEDGEMENTS: This investigation was supported by grants from the National Institutes of Health, USPHS (AM-14574 and -14575) and the American Heart Association, Inc. (#73,840). H.M.M. was supported by a Postdoctoral Fellowshi~ from the National Institutes of Health, and D.S. by the Insurance Medical Scientist Scholarship Fund.

PY - 1976/3/8

Y1 - 1976/3/8

N2 - By controlling conditions which affect the relative rates of the partial reactions in HMG-CoA synthesis, it has been possible to trap and partially characterize HMG (-SCoA)-S-enzyme, the postulated central intermediate in catalysis. At -25° in 25% ethanol, the breakdown of HMG (-SCoA)-S-enzyme to HMG-SCoA and HS-enzyme is slowed relative to its rate of formation from acetoacetyl-SCoA and acetyl-S-enzyme. Under these conditions label from acetoacetyl-S[3H]CoA or [14C]acetyl-S-enzyme can be trapped in the accumulated intermediate with [14C] activity appearing in the HMG moiety.

AB - By controlling conditions which affect the relative rates of the partial reactions in HMG-CoA synthesis, it has been possible to trap and partially characterize HMG (-SCoA)-S-enzyme, the postulated central intermediate in catalysis. At -25° in 25% ethanol, the breakdown of HMG (-SCoA)-S-enzyme to HMG-SCoA and HS-enzyme is slowed relative to its rate of formation from acetoacetyl-SCoA and acetyl-S-enzyme. Under these conditions label from acetoacetyl-S[3H]CoA or [14C]acetyl-S-enzyme can be trapped in the accumulated intermediate with [14C] activity appearing in the HMG moiety.

UR - http://www.scopus.com/inward/record.url?scp=0017264991&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017264991&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(76)80277-X

DO - 10.1016/S0006-291X(76)80277-X

M3 - Article

C2 - 4073

AN - SCOPUS:0017264991

SN - 0006-291X

VL - 69

SP - 92

EP - 98

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Trapping of a novel coenzyme a containing intermediate of 3-hydroxy-3-methylglutaryl-CoA synthase

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this