Hyperthermophilic aldolases as biocatalyst for C–C bond formation: rhamnulose 1-phosphate aldolase from Thermotoga maritima

Applied Microbiology and Biotechnology

Volumn 99, Issue 7, 2015, Pages 3057-3068

  Oroz Guinea, Isabel ^a   Sánchez Moreno, Israel ^a   Mena, Montaña ^b   García Junceda, Eduardo ^a  

^a INSTITUTO DE QUÍMICA ORGÁNICA GENERAL   (Spain)

^b Facultad de Ciencias Ambientales y Bioquimica   (Spain)

Author keywords

Aldolases; Biocatalysis; Enzyme catalysis; Hyperthermophilic enzymes; Thermostability; Thermozyme

Indexed keywords

CATALYSIS; CHEMICAL BONDS; CLONING; ESCHERICHIA COLI; GENES; METAL IONS; METALS;

ALDOLASES; BIOCATALYSIS; ENZYME CATALYSIS; HYPERTHERMOPHILIC; THERMOSTABILITY; THERMOZYMES;

ENZYMES;

BACTERIAL ENZYME; RHAMNULOSE 1 PHOSPHATE ALDOLASE; UNCLASSIFIED DRUG; ZINC; LYASE; RECOMBINANT PROTEIN; RHAMNULOSE-1-PHOSPHATE ADOLASE;

BACTERIUM; CATALYSIS; CATALYST; CHEMICAL BONDING; ENZYME ACTIVITY; MARINE TECHNOLOGY; REACTION KINETICS;

ALDOL REACTION; ARTICLE; BACTERIAL CELL; BIOCATALYST; CARBON BOND; CARBON NUCLEAR MAGNETIC RESONANCE; CHEMICAL BOND; CONTROLLED STUDY; ENZYMATIC DEGRADATION; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STABILITY; ESCHERICHIA COLI; HETEROLOGOUS EXPRESSION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYPERTHERMOPHILIC BACTERIUM; NONHUMAN; PH MEASUREMENT; PROTEIN QUATERNARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; ROOM TEMPERATURE; THERMOSTABILITY; THERMOTOGA MARITIMA; AMINO ACID SEQUENCE; CATALYSIS; CHEMISTRY; ENZYMOLOGY; GENETICS; HALF LIFE TIME; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PH; TEMPERATURE;

ESCHERICHIA COLI; THERMOTOGA MARITIMA;

ALDEHYDE-LYASES; AMINO ACID SEQUENCE; CATALYSIS; CLONING, MOLECULAR; ENZYME STABILITY; ESCHERICHIA COLI; HALF-LIFE; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; TEMPERATURE; THERMOTOGA MARITIMA;

EID: 84925014175     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-6123-7     Document Type: Article

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