TK1299, a highly thermostable NAD(P)H oxidase from Thermococcus kodakaraensis exhibiting higher enzymatic activity with NADPH

Journal of Bioscience and Bioengineering

Volumn 116, Issue 1, 2013, Pages 39-44

  Nisar, Muhammad Atif ^a   Rashid, Naeem ^a   Bashir, Qamar ^a   Gardner, Qurra tul Ann Afza ^a   Shafiq, Muhammad Hassan ^a   Akhtar, Muhammad ^a,b  

^a UNIVERSITY OF THE PUNJAB   (Pakistan)

^b UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

Author keywords

Circular dichroism; Cloning; Hyperthermophile; NAD(P)H oxidase; Thermococcus kodakaraensis; Thermostable

Indexed keywords

GEL-FILTRATION CHROMATOGRAPHY; HYPERTHERMOPHILES; MATRIX-ASSISTED LASER DESORPTION/IONIZATION TIME-OF-FLIGHT; MOLECULAR PROPERTIES; NAD(P)H; NICOTINAMIDE ADENINE DINUCLEOTIDES; THERMOCOCCUS KODAKARAENSIS; THERMOSTABLE;

AMINO ACIDS; CLONING; DICHROISM; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; GENE ENCODING; RECOMBINANT PROTEINS;

ENZYME ACTIVITY;

AMINO ACID; FLAVINE ADENINE NUCLEOTIDE; OXYGEN; POLYPEPTIDE; QUERCETIN; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TK1299 PROTEIN; UNCLASSIFIED DRUG; WATER;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; ESCHERICHIA COLI; GEL FILTRATION CHROMATOGRAPHY; GENE EXPRESSION; GENE PRODUCT; INCUBATION TIME; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; PH; PHYLOGENETIC TREE; PROTEIN QUATERNARY STRUCTURE; SEQUENCE ANALYSIS; STRUCTURAL GENE; THERMOCOCCUS KODAKARENSIS;

AMINO ACID SEQUENCE; DINITROCRESOLS; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; NADP; NADPH OXIDASE; OXIDATION-REDUCTION; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE; THERMOCOCCUS;

ESCHERICHIA COLI; THERMOCOCCUS KODAKARENSIS;

EID: 84878170534     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2013.01.020     Document Type: Article

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