SCOPUS 정보 검색 플랫폼

Volumn 40, Issue 12, 2001, Pages 3657-3665

Direct measurement of acylenzyme hydrolysis demonstrates rate-limiting deacylation in cleavage of physiological sequences by the processing protease Kex2

(2) Rockwell, N C a,b,c Fuller, R S c

a STANFORD UNIVERSITY (United States)

b UNIVERSITY OF CALIFORNIA (United States)

c UNIVERSITY OF MICHIGAN HEALTH SYSTEM (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CLEAVAGE; PHYSIOLOGICAL SEQUENCES;

ACYLATION; CHEMICAL BONDS; DEGRADATION; ENZYME KINETICS; ENZYMES; PHYSIOLOGY; THERMOANALYSIS; YEAST;

HYDROLYSIS;

7 AMINO 4 METHYLCOUMARIN; AMIDE; COUMARIN DERIVATIVE; ESTER; FURIN; ISOTOPE; SERINE PROTEINASE; SERINE PROTEINASE KEX 2; SUBTILISIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; DEACYLATION; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; SACCHAROMYCES CEREVISIAE;

ACYLATION; AMIDES; CHROMOGENIC COMPOUNDS; COUMARINS; DEUTERIUM; HYDROLYSIS; KINETICS; MASS SPECTROMETRY; OLIGOPEPTIDES; PROPROTEIN CONVERTASES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SOLVENTS; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; SUBTILISINS; TEMPERATURE;

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 0035957281 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi0020877 Document Type: Article

Times cited : (21)

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