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EC 4.2.1.104

EC 4.2.1.104

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system. Most BioCyc compounds have.
a recycling substrate [2]. History. EC created 1972 as EC transferred 1990 to EC transferred 2001 to EC, modified.
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated. Most BioCyc compounds.

EC 4.2.1.104 - free

Reaction of the N-terminal methionine residues in cyanase with diethylpyrocarbonate. Commercial use or download access requires a license. The carbamate spontaneously hydrolyses to ammonia and carbon dioxide. Transcriptional regulation and expression pattern of AtCYN, overview. Fusarium oxysporum species complex. Bicarbonate functions as a recycling substrate.. Reaction of the N-terminal methionine residues in cyanase with diethylpyrocarbonate. Bicarbonate is a recycling substrate for cyanase. The ec parameter has to be set to be able to search for an EC. Purification and properties of the inducible enzyme cyanase. Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. The expected taxonomic range EC 4.2.1.104 this enzyme EC 4.2.1.104 Eukaryota, Bacteria. EC 4.2.1.104

EC 4.2.1.104 - discography

View entry in raw text format no links. Bicarbonate functions as a recycling substrate.. Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. PATHWAY BRENDA Link KEGG Link MetaCyc Link. Its mechanism is to catalyse the attack of bicarbonate on cyanate, with elimination of carbon dioxide, thus catalysing hydration of the cyanate to carbamae. Purification and properties of the inducible enzyme cyanase.