An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates

Biochemical Journal

Volumn 343, Issue 3, 1999, Pages 563-570

  Buchanan, Catriona L ^a   Connaris, Helen ^a   Danson, Michael J ^a   Reeve, Christopher D ^b   Hough, David W ^a  

^a University of Bath   (United Kingdom)

^b Avecia LifeScience Molecules   (United Kingdom)

Author keywords

2 Keto 3 deoxygluconate; Biotransformation; C C bond

Indexed keywords

BACTERIAL ENZYME; FRUCTOSE BISPHOSPHATE ALDOLASE; SIALIDASE; SODIUM BOROHYDRIDE;

AMINO ACID SEQUENCE; ARTICLE; BIOTRANSFORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SUBSTRATE; GENE SEQUENCE; HALF LIFE TIME; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SULFOLOBUS SOLFATARICUS; TEMPERATURE SENSITIVITY; THERMOSTABILITY;

ALDEHYDE-LYASES; AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BASE SEQUENCE; CHROMATOGRAPHY, ION EXCHANGE; CLONING, MOLECULAR; ENZYME STABILITY; ESCHERICHIA COLI; HAEMOPHILUS INFLUENZAE; HEAT; KINETICS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; SULFOLOBUS; THERMODYNAMICS;

ARCHAEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; SULFOLOBUS SOLFATARICUS;

EID: 0033229936     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3430563     Document Type: Article

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