Evolution of lactate dehydrogenase-A homologs of barracuda fishes (genus Sphyraena) from different thermal environments: Differences in kinetic properties and thermal stability are due to amino acid substitutions outside the active site

Biochemistry

Volumn 36, Issue 11, 1997, Pages 3207-3215

  Holland, Linda Z ^a   McFall Ngai, Margaret ^b   Somero, George N ^c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF HAWAII   (United States)

^c STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LACTATE DEHYDROGENASE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING AFFINITY; DNA SEQUENCE; ENZYME PURIFICATION; EVOLUTION; FISH; GENE AMPLIFICATION; MICHAELIS CONSTANT; NONHUMAN; PEPTIDE MAPPING; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; THERMAL ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BINDING SITES; CATTLE; CHICKENS; DOGFISH; ENZYME STABILITY; EVOLUTION; FISHES; ISOENZYMES; KINETICS; L-LACTATE DEHYDROGENASE; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; MUTAGENESIS, SITE-DIRECTED; PEPTIDE MAPPING; POLYMERASE CHAIN REACTION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE; THERMODYNAMICS; VARIATION (GENETICS);

ANIMALIA; PISCES; SPHYRAENA; SPHYRAENA ARGENTEA; SPHYRAENA IDIASTES; SPHYRAENA LUCASANA;

EID: 0030896384     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962664k     Document Type: Article

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