1h54
From Proteopedia
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MALTOSE PHOSPHORYLASE FROM LACTOBACILLUS BREVIS
Overview
BACKGROUND: Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes, the conversion of maltose and inorganic phosphate into, beta-D-glucose-1-phosphate and glucose without requiring any cofactors, such as pyridoxal phosphate. The enzyme is part of operons that are, involved in maltose/malto-oligosaccharide metabolism. Maltose, phosphorylases have been classified in family 65 of the glycoside, hydrolases. No structure is available for any member of this family., RESULTS: We report here the 2.15 A resolution crystal structure of the MP, from Lactobacillus brevis in complex with the cosubstrate phosphate. This, represents the first structure of a disaccharide phosphorylase. The, structure consists of an N-terminal complex beta sandwich domain, a, helical linker, an (alpha/alpha)6 ... [(full description)]
About this Structure
1H54 is a [Single protein] structure of sequence from [Lactobacillus brevis] with K and PO4 as [ligands]. Active as [Maltose phosphorylase], with EC number [2.4.1.8]. Structure known Active Sites: KA, KB and PO4. Full crystallographic information is available from [OCA].
Reference
Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases., Egloff MP, Uppenberg J, Haalck L, van Tilbeurgh H, Structure. 2001 Aug;9(8):689-97. PMID:11587643
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