Biomaterial Database

Studies of enzyme-catalyzed modification of proteins. I. Tyrosinase-catalyzed modification of asparaginase. 1976

M Tokushige, and F Moriya

Asparaginase [EC 3.5.1.1.] of Escherichia coli, an anti-tumor enzyme, was inactivated in a time-dependent fashion by mushroom tyrosinase [EC1.14.18.1.]. The inactivation did not proceed, however, when heat-inactivated tyrosinase was used. Exculusion of the atmospheric oxygen or addition of diethyldithiocarbamate, a copper selective chelating agent, prevented the inactivation. The difference absorption spectrum of tyrosinase-inactivated asparaginase versus intact asparaginase exhibited the appearance of marked absorption peaks at 300 and 350 nm. These results indicate that the tyrosyl residue(s) of asparaginase, which is essential for the activity is enzymatically modified by tyrosianes.

UI	MeSH Term	Description	Entries
D010101	Oxygen Consumption	The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)	Consumption, Oxygen,Consumptions, Oxygen,Oxygen Consumptions
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D011489	Protein Denaturation	Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.	Denaturation, Protein,Denaturations, Protein,Protein Denaturations
D004125	Dimethyldithiocarbamate	A chemical that acts as a dopamine beta-hydroxylase inhibitor. Its salts are agricultural fungicides. It is inferior to diethyldithiocarbamate as a chelating agent.
D004156	Catechol Oxidase	An enzyme of the oxidoreductase class that catalyzes the reaction between catechol and oxygen to yield benzoquinone and water. It is a complex of copper-containing proteins that acts also on a variety of substituted catechols. EC 1.10.3.1.	Diphenol Oxidases,Diphenol Oxidase,Polyphenol Oxidase,Polyphenoloxidase,Oxidase, Catechol,Oxidase, Diphenol,Oxidase, Polyphenol,Oxidases, Diphenol
D004926	Escherichia coli	A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.	Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D001215	Asparaginase	A hydrolase enzyme that converts L-asparagine and water to L-aspartate and NH3. EC 3.5.1.1.	Asparaginase II,Asparaginase medac,Asparagine Deaminase,Colaspase,Crasnitin,Elspar,Erwinase,Kidrolase,Leunase,Paronal,Deaminase, Asparagine,medac, Asparaginase

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