Chemical modification of NADP-isocitrate dehydrogenase from Cephalosporium acremonium evidence of essential histidine and lysine groups at the active site (Q77363179)

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scientific article published on 01 May 1999

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English	Chemical modification of NADP-isocitrate dehydrogenase from Cephalosporium acremonium evidence of essential histidine and lysine groups at the active site	scientific article published on 01 May 1999

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scholarly article

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5 December 2019

Chemical modification of NADP-isocitrate dehydrogenase from Cephalosporium acremonium evidence of essential histidine and lysine groups at the active site (English)

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5 December 2019

Cephalosporium acremonium

object named as

Cephalosporium acremonium

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J Olano

1

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5 December 2019

J Soler

2

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5 December 2019

F Busto

3

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5 December 2019

D De Arriaga

4

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5 December 2019

publication date

1 May 1999

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5 December 2019

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5 December 2019

261

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5 December 2019

3

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5 December 2019

640-649

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5 December 2019

Affinity labels and spectroscopic probes of porcine heart NADP-dependent isocitrate dehydrogenase

1 reference

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alpha-Oxoglutarate as a precursor of the D-alpha-aminoadipic acid residue in cephalosporin C.

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Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase

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Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes

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Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-A resolution: a pseudo-Michaelis ternary complex

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Isolation and sequence of a cDNA encoding porcine mitochondrial NADP-specific isocitrate dehydrogenase

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Ionization of isocitrate bound to pig heart NADP+-dependent isocitrate dehydrogenase: 13C NMR study of substrate binding

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Identification of adenine binding domain peptides of the NADP+ active site within porcine heart NADP(+)-dependent isocitrate dehydrogenase

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N-ethylmaleimide profiling of yeast NADP-dependent isocitrate dehydrogenase.

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Inactivation of pig heart NADP-specific isocitrate dehydrogenase by two affinity reagents is due to reaction with a cysteine not essential for function

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal 5′-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity

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Evidence for an essential histidine residue in S-adenosylhomocysteinase from rat liver

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Evidence of an essential histidine residue in thermolysin.

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Ionic properties of an essential histidine residue in pig heart lactate dehydrogenase

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Coenzyme binding by native and chemically modified pig heart triphosphopyridine nucleotide dependent isocitrate dehydrogenase

1 reference

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21 January 2018

Equilibrium binding of coenzymes and substrates to nicotinamide-adenine dinucleotide phosphate-linked isocitrate dehydrogenase from bovine heart mitochondria

1 reference

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21 January 2018

Spectroscopic studies of the interactions of coenzymes and coenzyme fragments with pig heart, oxidized triphosphopyridine nucleotide specific isocitrate dehydrogenase

1 reference

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21 January 2018

41 Modification of histidyl residues in proteins by diethylpyrocarbonate

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21 January 2018

Histidine in the Nucleotide-Binding Site of NADP-Linked Isocitrate Dehydrogenase from Pig Heart

1 reference

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21 January 2018

Evidence for an essential histidine residue in d-xylose isomerases

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21 January 2018

Chemical modification of bacterial luciferase with ethoxyformic anhydride: evidence for an essential histidyl residue

1 reference

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21 January 2018

Isocitrate lyase from Cephalosporium acremonium. Role of Mg2+ ions, kinetics, and evidence for a histidine residue in the active site of the enzyme

1 reference

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21 January 2018

Ethoxyformylation of proteins. Reaction of ethoxyformic anhydride with .alpha.-chymotrypsin, pepsin, and pancreatic ribonuclease at pH 4

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Chemical modification of 3 alpha,20 beta-hydroxysteroid dehydrogenase with diethyl pyrocarbonate. Evidence for an essential, highly reactive, lysyl residue

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Site-directed mutagenesis and chemical modification of histidine residues on an alpha-class chick liver glutathione S-transferase CL 3-3. Histidines are not needed for the activity of the enzyme and diethylpyrocarbonate modifies both histidine and l

1 reference

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Evidence for an essential lysyl residue in phospholipase D from Streptomyces sp. by modification with diethyl pyrocarbonate and pyridoxal 5-phosphate

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Inactivation of Phycomyces isocitrate lyase by thiol-reactive reagents. Evidence for an essential thiol group

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Kinetic mechanism of Escherichia coli isocitrate dehydrogenase.

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Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP(+)-dependent isocitrate dehydrogenase from Escherichia coli

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Identifiers

10.1046/J.1432-1327.1999.00297.X

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10215879%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10215879%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

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