Involvement of the conserved histidine-188 residue in the L-lactate dehydrogenase from Thermus caldophilus GK24 in allosteric regulation by fructose 1,6-bisphosphate (Q68388486)

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scientific article published on 01 May 1988

Language	Label	Description	Also known as
English	Involvement of the conserved histidine-188 residue in the L-lactate dehydrogenase from Thermus caldophilus GK24 in allosteric regulation by fructose 1,6-bisphosphate	scientific article published on 01 May 1988

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scholarly article

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24 September 2019

Involvement of the conserved histidine-188 residue in the L-lactate dehydrogenase from Thermus caldophilus GK24 in allosteric regulation by fructose 1,6-bisphosphate (English)

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24 September 2019

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G Schroeder

1

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24 September 2019

H Matsuzawa

2

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24 September 2019

T Ohta

3

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24 September 2019

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publication date

1 May 1988

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24 September 2019

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6

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Biochemical and Biophysical Research Communications

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24 September 2019

152

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24 September 2019

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24 September 2019

1236-1241

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24 September 2019

Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium.

1 reference

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L-Lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium. Desensitization to fructose 1,6-bisphosphate in the activated state by arginine-specific chemical modification and the N-terminal amino acid sequence.

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Fructose 1,6-bisphosphate-dependent L-lactate dehydrogenase from Thermus aquaticus YT-1, an extreme thermophile: activation by citrate and modification reagents and comparison with Thermus caldophilus GK24 L-lactate dehydrogenase

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Nucleotide sequence and characteristics of the gene for L-lactate dehydrogenase of Thermus caldophilus GK24 and the deduced amino-acid sequence of the enzyme

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Comparative studies of lactic acid dehydrogenases in lactic acid bacteria. I. Purification and kinetics of the allosteric L-lactic acid dehydrogenase from Lactobacillus casei ssp. casei and Lactobacillus curvatus

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FRUCTOSE-1,6-DIPHOSPHATE REQUIREMENT OF STREPTOCOCCAL LACTIC DEHYDROGENASES

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The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei

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Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. III) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Hydroxylamine-, o-iodosobenzoic acid- and tryptic-fragme

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Crystallization of lactate dehydrogenase from Bacillus stearothermophilus

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Affinity labelling of the allosteric site of the L-lactate dehydrogenase of Lactobacillus casei

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Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis

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Structure and Function of L-Lactate Dehydrogenases from Thermophilic and Mesophilic Bacteria. I) Isolation and Characterization of Lactate Dehydrogenases from Thermophilic and Mesophilic Bacilli

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Fructose 1,6-diphosphate-activated L-lactate dehydrogenase from Streptococcus lactis: kinetic properties and factors affecting activation

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Identifiers

10.1016/S0006-291X(88)80417-0

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:3377774%20AND%20SRC:MED&resulttype=core&format=json

24 September 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:3377774%20AND%20SRC:MED&resulttype=core&format=json

24 September 2019

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