2ber | pdb_00002ber
Y370G ACTIVE SITE MUTANT OF THE SIALIDASE FROM MICROMONOSPORA VIRIDIFACIENS IN COMPLEX WITH BETA-NEU5AC (SIALIC ACID).
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Overview
Mutagenesis of the conserved tyrosine (Y370) of the Micromonospora, viridifaciens sialidase to small amino acids changes the mechanism of, catalysis from retention of anomeric configuration to inversion [Watson, J. N., et al. (2003) Biochemistry 42, 12682-12690]. For the Y370G mutant, enzyme-catalyzed hydrolysis of a series of aryl sialosides and, 3'-sialyllactose, the derived Bronsted parameters (beta(lg)) on k(cat) and, k(cat)/K(m) are -0.63 +/- 0.05 and -0.80 +/- 0.08, respectively. Thus, for, the Y370G enzyme, glycosidic C-O bond cleavage is rate-determining., Analysis of the activity of the Y370G mutant and wild-type enzymes against, a substrate [3,4-dihydro-2H-pyrano[3,2-c]pyridinium, alpha-d-N-acetylneuraminide (DHP-alphaNeu5Ac)] whose hydrolysis cannot be, accelerated by acid ... [(full description)]
About this Structure
2BER is a [Single protein] structure of sequence from [Micromonospora viridifaciens] with SLB and NA as [ligands]. Active as [[1]], with EC number [3.2.1.18]. Full crystallographic information is available from [OCA].
Reference
Structure and mechanism of action of an inverting mutant sialidase., Newstead S, Watson JN, Knoll TL, Bennet AJ, Taylor G, Biochemistry. 2005 Jun 28;44(25):9117-22. PMID:15966735
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