Arginine Deiminase (Paperback)


Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. In enzymology, an arginine deiminase (EC 3.5.3.6) is an enzyme that catalyzes the chemical reaction L-arginine + H2O \rightleftharpoons L-citrulline + NH3. Thus, the two substrates of this enzyme are L-arginine and H2O, whereas its two products are L-citrulline and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is L-arginine iminohydrolase. Other names in common use include arginine dihydrolase, citrulline iminase, and L-arginine deiminase. This enzyme participates in arginine and proline metabolism.

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Product Description

Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. In enzymology, an arginine deiminase (EC 3.5.3.6) is an enzyme that catalyzes the chemical reaction L-arginine + H2O \rightleftharpoons L-citrulline + NH3. Thus, the two substrates of this enzyme are L-arginine and H2O, whereas its two products are L-citrulline and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is L-arginine iminohydrolase. Other names in common use include arginine dihydrolase, citrulline iminase, and L-arginine deiminase. This enzyme participates in arginine and proline metabolism.

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Product Details

General

Imprint

Crypt Publishing

Country of origin

United States

Release date

December 2011

Availability

Supplier out of stock. If you add this item to your wish list we will let you know when it becomes available.

First published

December 2011

Editors

Dimensions

229 x 152 x 5mm (L x W x T)

Format

Paperback - Trade

Pages

88

ISBN-13

978-6200025302

Barcode

9786200025302

Categories

LSN

6200025304



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