The roles of Tyr91 and Lys162 in general acid-base catalysis in the pigeon NADP+-dependent malic enzyme

Biochemical Journal

Volumn 411, Issue 3, 2008, Pages 467-473

  Kuo, Cheng Chin ^a   Lin, Kuan Yu ^b   Hsu, Yau Jung ^b   Lin, Shu Yu ^b   Lin, Yu Tsen ^b   Chang, Gu Gang ^c   Chou, Wei Yuan ^b  

^a NATIONAL HEALTH RESEARCH INSTITUTES   (Taiwan)

^b NATIONAL DEFENSE MEDICAL CENTER   (Taiwan)

^c NATIONAL YANG MING UNIVERSITY   (Taiwan)

Author keywords

Chemical rescue; Enol keto tautomerization; General acid base catalysis; Malic enzyme; pH profile; Site directed mutagenesis

Indexed keywords

AMMONIUM COMPOUNDS; CARBOXYLATION; ENZYME ACTIVITY; HYDROGEN BONDS; PH EFFECTS;

ENOL-KETO TAUTOMERIZATION; GENERAL ACID-BASE CATALYSIS; SITE-DIRECTED MUTAGENESIS;

CATALYST ACTIVITY;

AMMONIUM CHLORIDE; LYSINE; MALATE DEHYDROGENASE (NADP); MALIC ACID; OXALOACETIC ACID; OXIDOREDUCTASE; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TYROSINE; ACID; ALKALI; MALATE DEHYDROGENASE; MALATE DEHYDROGENASE (OXALOACETATE DECARBOXYLATING) (NADP+); MALATE DEHYDROGENASE (OXALOACETATE-DECARBOXYLATING) (NADP+); NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ACID BASE BALANCE; ARTICLE; CATALYSIS; DECARBOXYLATION; ENZYME ACTIVITY; ENZYME MECHANISM; MUTANT; PIGEON; PKA; PRIORITY JOURNAL; PROTON TRANSPORT; REDUCTION; SITE DIRECTED MUTAGENESIS; STEADY STATE; WILD TYPE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; ENZYME ACTIVATION; ENZYME SPECIFICITY; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MUTATION; OXIDATION REDUCTION REACTION; PH;

COLUMBA;

ACIDS; ALKALIES; CATALYSIS; CIRCULAR DICHROISM; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; KINETICS; LYSINE; MALATE DEHYDROGENASE; MOLECULAR STRUCTURE; MUTATION; NADP; OXIDATION-REDUCTION; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TYROSINE;

EID: 42449100760     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071278     Document Type: Article

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