Purification and properties of extremely thermostable glutamate dehydrogenases from two hyperthermophilic archaebacteria, Pyrococcus woesei and Pyrococcus furiosus

Glutamate dehydrogenase (L-glutamate: NADP oxidoreductase, deaminating, EC 1.4.1.4) from the hyperthermophilic archaebacteria Pyrococcus woesei and P. furiosus were purified to homogeneity from crude extracts. The enzymes had similar enzymological properties: molecular mass, subunit structure, optim...

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Bibliographic Details
Published in:	Bioscience, biotechnology, and biochemistry Vol. 57; no. 6; pp. 945 - 951
Main Authors:	Ohshima, T. (Kyoto Univ. of Education (Japan)), Nishida, N
Format:	Journal Article
Language:	English
Published:	England Taylor & Francis 1993 Oxford University Press
Subjects:	Amino Acid Sequence Amino Acids - metabolism Archaea - enzymology BACTERIA Biotechnology CHEMICAL STRUCTURE CHEMICOPHYSICAL PROPERTIES Electrophoresis, Polyacrylamide Gel Enzyme Stability ESTRUCTURA QUIMICA GLUTAMATE DEHYDROGENASE Glutamate Dehydrogenase - chemistry Glutamate Dehydrogenase - isolation & purification Glutamate Dehydrogenase - metabolism GLUTAMATE DESHYDROGENASE GLUTAMATO DEHIDROGENASA Hydrogen-Ion Concentration Keto Acids - metabolism Kinetics Marine MICROORGANISME THERMOPHILE MICROORGANISMOS TERMOFILOS Molecular Sequence Data Molecular Weight NAD - metabolism NADP - metabolism PROPIEDADES FISICO-QUIMICAS PROPRIETE PHYSICOCHIMIQUE PURIFICACION PURIFICATION Pyrococcus furiosus Pyrococcus woesei RESISTANCE A LA TEMPERATURE RESISTENCIA A LA TEMPERATURA STRUCTURE CHIMIQUE Substrate Specificity Temperature TEMPERATURE RESISTANCE THERMOPHILIC MICROORGANISMS
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Summary:	Glutamate dehydrogenase (L-glutamate: NADP oxidoreductase, deaminating, EC 1.4.1.4) from the hyperthermophilic archaebacteria Pyrococcus woesei and P. furiosus were purified to homogeneity from crude extracts. The enzymes had similar enzymological properties: molecular mass, subunit structure, optimum pHs for the oxidative deamination and reductive amination, substrate specificity and coenzyme specificity as well as thermostability; the activity was not lost after incubation at 105°C for 30 min. However, some differences were detected in resistance to urea denaturation and effects of salts on their activity and stability. The N-terminal 20 amino acid sequences of the two enzymes were identical.
Bibliography:	F60 Q02 9402357 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0916-8451 1347-6947
DOI:	10.1271/bbb.57.945