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1h54
From Proteopedia
(New page: 200px<br /> <applet load="1h54" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h54, resolution 2.15Å" /> '''MALTOSE PHOSPHORYLA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1H54 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Lactobacillus_brevis Lactobacillus brevis]] with K and PO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.8 2.4.1.8]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H54 OCA]]. | + | 1H54 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Lactobacillus_brevis Lactobacillus brevis]] with K and PO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Maltose_phosphorylase Maltose phosphorylase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.8 2.4.1.8]]. Structure known Active Sites: KA, KB and PO4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H54 OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11587643 11587643] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11587643 11587643] | ||
[[Category: Lactobacillus brevis]] | [[Category: Lactobacillus brevis]] | ||
| + | [[Category: Maltose phosphorylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Egloff, M.P.]] | [[Category: Egloff, M.P.]] | ||
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[[Category: maltose metabolism]] | [[Category: maltose metabolism]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:35:37 2007'' |
Revision as of 09:30, 30 October 2007
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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
Page seeded by OCA on Tue Oct 30 11:35:37 2007
