Essential arginyl residues in yeast enolase

C. L. Borders; Mary L. Woodall; Alfred L. George

doi:10.1016/0006-291X(78)90868-9

Essential arginyl residues in yeast enolase

C. L. Borders^*, Mary L. Woodall, Alfred L. George

^*Corresponding author for this work

Pharmacology

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

19 Scopus citations

Abstract

Yeast enolase is rapidly inactivated by butanedione in borate buffer, complete inactivation correlating with the modification of 1. 8 arginyl residues per subunit. Protection against inactivation is provided by either an equilibrium mixture of substrates or inorganic phosphate, a competitive inhibitor of the enzyme. Complete protection by substrates correlates with the shielding of 1. 3 arginyl residues per subunit, while phosphate protects 1. 0 arginyl residue per subunit from modification.

Original language	English (US)
Pages (from-to)	901-906
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	82
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(78)90868-9
State	Published - Jun 14 1978

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/0006-291X(78)90868-9

Fingerprint Dive into the research topics of 'Essential arginyl residues in yeast enolase'. Together they form a unique fingerprint.

Cite this

@article{daf6cc5372194c368533e4a5ddc5959f,

title = "Essential arginyl residues in yeast enolase",

abstract = "Yeast enolase is rapidly inactivated by butanedione in borate buffer, complete inactivation correlating with the modification of 1. 8 arginyl residues per subunit. Protection against inactivation is provided by either an equilibrium mixture of substrates or inorganic phosphate, a competitive inhibitor of the enzyme. Complete protection by substrates correlates with the shielding of 1. 3 arginyl residues per subunit, while phosphate protects 1. 0 arginyl residue per subunit from modification.",

author = "Borders, {C. L.} and Woodall, {Mary L.} and George, {Alfred L.}",

year = "1978",

month = jun,

day = "14",

doi = "10.1016/0006-291X(78)90868-9",

language = "English (US)",

volume = "82",

pages = "901--906",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Essential arginyl residues in yeast enolase

AU - Borders, C. L.

AU - Woodall, Mary L.

AU - George, Alfred L.

PY - 1978/6/14

Y1 - 1978/6/14

N2 - Yeast enolase is rapidly inactivated by butanedione in borate buffer, complete inactivation correlating with the modification of 1. 8 arginyl residues per subunit. Protection against inactivation is provided by either an equilibrium mixture of substrates or inorganic phosphate, a competitive inhibitor of the enzyme. Complete protection by substrates correlates with the shielding of 1. 3 arginyl residues per subunit, while phosphate protects 1. 0 arginyl residue per subunit from modification.

AB - Yeast enolase is rapidly inactivated by butanedione in borate buffer, complete inactivation correlating with the modification of 1. 8 arginyl residues per subunit. Protection against inactivation is provided by either an equilibrium mixture of substrates or inorganic phosphate, a competitive inhibitor of the enzyme. Complete protection by substrates correlates with the shielding of 1. 3 arginyl residues per subunit, while phosphate protects 1. 0 arginyl residue per subunit from modification.

UR - http://www.scopus.com/inward/record.url?scp=0017847832&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017847832&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(78)90868-9

DO - 10.1016/0006-291X(78)90868-9

M3 - Article

C2 - 358969

AN - SCOPUS:0017847832

VL - 82

SP - 901

EP - 906

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -