(Q54579225)

1 June 2018

title

Allosteric activation of L-lactate dehydrogenase analyzed by hybrid enzymes with effector-sensitive and -insensitive subunits. (English)

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1 June 2018

author

Shinya Fushinobu

1

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1 June 2018

author name string

Kamata K

2

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1 June 2018

Iwata S

3

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1 June 2018

Sakai H

4

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1 June 2018

Ohta T

5

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1 June 2018

Matsuzawa H

6

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1 June 2018

language of work or name

English

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publication date

1 October 1996

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1 June 2018

Journal of Biological Chemistry

published in

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1 June 2018

volume

271

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issue

41

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1 June 2018

page(s)

25611-25616

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1 June 2018

Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site.

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T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control

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Functional anion binding sites in dogfish M4 lactate dehydrogenase.

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

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Allosteric activation in Bacillus stearothermophilus lactate dehydrogenase investigated by an X-ray crystallographic analysis of a mutant designed to prevent tetramerization of the enzyme.

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Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase

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Transduction of binding energy into hemoglobin cooperativity

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Communication between catalytic subunits in hybrid aspartate transcarbamoylase molecules: effect of ligand binding to active chains on the conformation of unliganded, inactive chains

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Subunit communication in the anthranilate synthase complex from Salmonella typhimurium

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The use of subunit hybridization to monitor the reassociation of porcine lactate dehydrogenase after acid dissociation

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Identifiers

DOI

10.1074/JBC.271.41.25611

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1 June 2018

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1 June 2018