Dissecting the catalytic mechanism of staphylococcal lipases using carbamate substrates: Chain length selectivity, interfacial activation, and cofactor dependence

Biochemistry

Volumn 36, Issue 47, 1997, Pages 14539-14550

  Simons, Jan Willem F A ^b   Boots, Jan Willem P ^b   Kats, Mark P ^b   Slotboom, Arend J ^b   Egmond, Maarten R ^b   Verheij, Hubertus M ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CALCIUM; CARBAMIC ACID DERIVATIVE; TRIACYLGLYCEROL LIPASE;

ACYLATION; ARTICLE; CATALYSIS; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME STABILITY; MICELLE; NONHUMAN; PH; PRIORITY JOURNAL; STAPHYLOCOCCUS AUREUS;

CARBAMATES; CATALYSIS; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; KINETICS; LIPASE; MODELS, CHEMICAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SOLUBILITY; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS; SUBSTRATE SPECIFICITY; THERMODYNAMICS; UREA;

EID: 0030711518     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9713714     Document Type: Article

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