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Identification of a cysteine residue as the binding site for the dipyrromethane cofactor at the active site of Escherichia coli porphobilinogen deaminase

โœ Scribed by Peter M. Jordan; Martin J. Warren; Howard J. Williams; Neal J. Stolowich; Charles A. Roessner; Stephen K. Grant; A.Ian Scott


Book ID
115921251
Publisher
Elsevier Science
Year
1988
Tongue
English
Weight
442 KB
Volume
235
Category
Article
ISSN
0014-5793

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๐Ÿ“œ SIMILAR VOLUMES


Identification of arginine 331 as an imp
โœ Seema Qamar; Katherine Marsh; Alan Berry ๐Ÿ“‚ Article ๐Ÿ“… 2008 ๐Ÿ› Cold Spring Harbor Laboratory Press ๐ŸŒ English โš– 813 KB

## Abstract Treatment of the Class II fructoseโ€1,6โ€bisphosphate aldolase of __Escherichia coli__ with the arginineโ€specific ฮฑโ€dicarbonyl reagents, butanedione or phenylglyoxal, results in inactivation of the enzyme. The enzyme is protected from inactivation by the substrate, fructose 1,6โ€bisphospha