Occurrence of two different glutamate dehydrogenase activities in the halophilic bacterium Salinibacter ruber

Maria José Bonete; Francisco Pérez-Pomares; Susana Díaz; Juan Ferrer; Aharon Oren

doi:10.1016/S0378-1097(03)00592-5

Occurrence of two different glutamate dehydrogenase activities in the halophilic bacterium Salinibacter ruber

Maria José Bonete^*, Francisco Pérez-Pomares, Susana Díaz, Juan Ferrer, Aharon Oren

^*Corresponding author for this work

Department of Plant and Environmental Sciences (Natural Sciences)

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

18 Scopus citations

Abstract

Salinibacter ruber, an extremely halophilic member of the domain Bacteria, has two different cytoplasmic glutamate dehydrogenase activities, marked as GDHI and GDHII. GDHI showed a strong dependence on high salt concentrations for stability, but not for activity, displaying maximal activity in the absence of salts. GDHII depended on high salt concentrations for both activity and stability. It catalyzed amination of 2-oxoglutarate with optimal activity in 3 M KCl at pH 8. No activating effect was found when NaCl was replaced by KCl. Only GDHII displayed activity in the deamination reaction of glutamate with an optimal pH of 9.5. Both enzymes were activated by certain amino acids (L-leucine, L-histidine, L-phenylalanine) and by nucleotides such as ADP or ATP. A low-molecular-mass cytoplasmic fraction was found to be a highly effective activator of GDHII in the presence of high NaCl concentrations.

Original language	American English
Pages (from-to)	181-186
Number of pages	6
Journal	FEMS Microbiology Letters
Volume	226
Issue number	1
DOIs	https://doi.org/10.1016/S0378-1097(03)00592-5
State	Published - 12 Sep 2003

Bibliographical note

Funding Information:
This work was supported by funds from MCYT BIO2002-03197.

Keywords

Glutamate dehydrogenase
Halophilic enzyme
Salinibacter ruber

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10.1016/S0378-1097(03)00592-5

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title = "Occurrence of two different glutamate dehydrogenase activities in the halophilic bacterium Salinibacter ruber",

abstract = "Salinibacter ruber, an extremely halophilic member of the domain Bacteria, has two different cytoplasmic glutamate dehydrogenase activities, marked as GDHI and GDHII. GDHI showed a strong dependence on high salt concentrations for stability, but not for activity, displaying maximal activity in the absence of salts. GDHII depended on high salt concentrations for both activity and stability. It catalyzed amination of 2-oxoglutarate with optimal activity in 3 M KCl at pH 8. No activating effect was found when NaCl was replaced by KCl. Only GDHII displayed activity in the deamination reaction of glutamate with an optimal pH of 9.5. Both enzymes were activated by certain amino acids (L-leucine, L-histidine, L-phenylalanine) and by nucleotides such as ADP or ATP. A low-molecular-mass cytoplasmic fraction was found to be a highly effective activator of GDHII in the presence of high NaCl concentrations.",

keywords = "Glutamate dehydrogenase, Halophilic enzyme, Salinibacter ruber",

author = "Bonete, {Maria Jos{\'e}} and Francisco P{\'e}rez-Pomares and Susana D{\'i}az and Juan Ferrer and Aharon Oren",

note = "Funding Information: This work was supported by funds from MCYT BIO2002-03197.",

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doi = "10.1016/S0378-1097(03)00592-5",

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T1 - Occurrence of two different glutamate dehydrogenase activities in the halophilic bacterium Salinibacter ruber

AU - Bonete, Maria José

AU - Pérez-Pomares, Francisco

AU - Díaz, Susana

AU - Ferrer, Juan

AU - Oren, Aharon

N1 - Funding Information: This work was supported by funds from MCYT BIO2002-03197.

PY - 2003/9/12

Y1 - 2003/9/12

N2 - Salinibacter ruber, an extremely halophilic member of the domain Bacteria, has two different cytoplasmic glutamate dehydrogenase activities, marked as GDHI and GDHII. GDHI showed a strong dependence on high salt concentrations for stability, but not for activity, displaying maximal activity in the absence of salts. GDHII depended on high salt concentrations for both activity and stability. It catalyzed amination of 2-oxoglutarate with optimal activity in 3 M KCl at pH 8. No activating effect was found when NaCl was replaced by KCl. Only GDHII displayed activity in the deamination reaction of glutamate with an optimal pH of 9.5. Both enzymes were activated by certain amino acids (L-leucine, L-histidine, L-phenylalanine) and by nucleotides such as ADP or ATP. A low-molecular-mass cytoplasmic fraction was found to be a highly effective activator of GDHII in the presence of high NaCl concentrations.

AB - Salinibacter ruber, an extremely halophilic member of the domain Bacteria, has two different cytoplasmic glutamate dehydrogenase activities, marked as GDHI and GDHII. GDHI showed a strong dependence on high salt concentrations for stability, but not for activity, displaying maximal activity in the absence of salts. GDHII depended on high salt concentrations for both activity and stability. It catalyzed amination of 2-oxoglutarate with optimal activity in 3 M KCl at pH 8. No activating effect was found when NaCl was replaced by KCl. Only GDHII displayed activity in the deamination reaction of glutamate with an optimal pH of 9.5. Both enzymes were activated by certain amino acids (L-leucine, L-histidine, L-phenylalanine) and by nucleotides such as ADP or ATP. A low-molecular-mass cytoplasmic fraction was found to be a highly effective activator of GDHII in the presence of high NaCl concentrations.

KW - Glutamate dehydrogenase

KW - Halophilic enzyme

KW - Salinibacter ruber

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U2 - 10.1016/S0378-1097(03)00592-5

DO - 10.1016/S0378-1097(03)00592-5

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AN - SCOPUS:0642369572

SN - 0378-1097

VL - 226

SP - 181

EP - 186

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 1

ER -

Occurrence of two different glutamate dehydrogenase activities in the halophilic bacterium Salinibacter ruber

Abstract

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Keywords

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