Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide dependent enzyme from Saccharomyces cerevisiae

R. J. Roon, H. L. Even, F. Larimore

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

A reduced nicotinamide adenine dinucleotide (NADH) dependent glutamate synthase has been detected and partially purified from crude extracts of Saccharomyces cerevisiae. The enzyme is specific for NADH, glutamine, and α ketoglutarate (Km values of 2.6 μM, 1.0 mM, and 140 μM, respectively) and has a pH optimum between 7.1 and 7.7. The stoichiometry of the reaction has been determined as 2 mol of glutamate synthesized per mol of glutamine consumed. Glutamate synthase can be distinguished from either of the glutamate dehydrogenases of yeast on the basis of its substrate requirements and behavior during agarose gel and ion exchange chromatography. Variations in the specific activity of glutamate synthase, which occur in response to changes in the growth medium, are similar in character to those observed with the nicotinamide adenine dinucleotide phosphate dependent (anabolic) glutamate dehydrogenase.

Original languageEnglish (US)
Pages (from-to)89-95
Number of pages7
JournalJournal of bacteriology
Volume118
Issue number1
StatePublished - Dec 1 1974

Fingerprint

Glutamate Synthase
Glutamate Dehydrogenase
Glutamine
NAD
Glutamate Synthase (NADH)
Saccharomyces cerevisiae
Ion Exchange Chromatography
Enzymes
Complex Mixtures
NADP
Sepharose
Glutamic Acid
Yeasts
Gels
Growth

Cite this

Glutamate synthase : properties of the reduced nicotinamide adenine dinucleotide dependent enzyme from Saccharomyces cerevisiae. / Roon, R. J.; Even, H. L.; Larimore, F.

In: Journal of bacteriology, Vol. 118, No. 1, 01.12.1974, p. 89-95.

Research output: Contribution to journalArticle

@article{5e53215875a84b2c9ba0e0085ab13a3b,
title = "Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide dependent enzyme from Saccharomyces cerevisiae",
abstract = "A reduced nicotinamide adenine dinucleotide (NADH) dependent glutamate synthase has been detected and partially purified from crude extracts of Saccharomyces cerevisiae. The enzyme is specific for NADH, glutamine, and α ketoglutarate (Km values of 2.6 μM, 1.0 mM, and 140 μM, respectively) and has a pH optimum between 7.1 and 7.7. The stoichiometry of the reaction has been determined as 2 mol of glutamate synthesized per mol of glutamine consumed. Glutamate synthase can be distinguished from either of the glutamate dehydrogenases of yeast on the basis of its substrate requirements and behavior during agarose gel and ion exchange chromatography. Variations in the specific activity of glutamate synthase, which occur in response to changes in the growth medium, are similar in character to those observed with the nicotinamide adenine dinucleotide phosphate dependent (anabolic) glutamate dehydrogenase.",
author = "Roon, {R. J.} and Even, {H. L.} and F. Larimore",
year = "1974",
month = "12",
day = "1",
language = "English (US)",
volume = "118",
pages = "89--95",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "1",

}

TY - JOUR

T1 - Glutamate synthase

T2 - properties of the reduced nicotinamide adenine dinucleotide dependent enzyme from Saccharomyces cerevisiae

AU - Roon, R. J.

AU - Even, H. L.

AU - Larimore, F.

PY - 1974/12/1

Y1 - 1974/12/1

N2 - A reduced nicotinamide adenine dinucleotide (NADH) dependent glutamate synthase has been detected and partially purified from crude extracts of Saccharomyces cerevisiae. The enzyme is specific for NADH, glutamine, and α ketoglutarate (Km values of 2.6 μM, 1.0 mM, and 140 μM, respectively) and has a pH optimum between 7.1 and 7.7. The stoichiometry of the reaction has been determined as 2 mol of glutamate synthesized per mol of glutamine consumed. Glutamate synthase can be distinguished from either of the glutamate dehydrogenases of yeast on the basis of its substrate requirements and behavior during agarose gel and ion exchange chromatography. Variations in the specific activity of glutamate synthase, which occur in response to changes in the growth medium, are similar in character to those observed with the nicotinamide adenine dinucleotide phosphate dependent (anabolic) glutamate dehydrogenase.

AB - A reduced nicotinamide adenine dinucleotide (NADH) dependent glutamate synthase has been detected and partially purified from crude extracts of Saccharomyces cerevisiae. The enzyme is specific for NADH, glutamine, and α ketoglutarate (Km values of 2.6 μM, 1.0 mM, and 140 μM, respectively) and has a pH optimum between 7.1 and 7.7. The stoichiometry of the reaction has been determined as 2 mol of glutamate synthesized per mol of glutamine consumed. Glutamate synthase can be distinguished from either of the glutamate dehydrogenases of yeast on the basis of its substrate requirements and behavior during agarose gel and ion exchange chromatography. Variations in the specific activity of glutamate synthase, which occur in response to changes in the growth medium, are similar in character to those observed with the nicotinamide adenine dinucleotide phosphate dependent (anabolic) glutamate dehydrogenase.

UR - http://www.scopus.com/inward/record.url?scp=0016365925&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016365925&partnerID=8YFLogxK

M3 - Article

C2 - 4362465

AN - SCOPUS:0016365925

VL - 118

SP - 89

EP - 95

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 1

ER -