1uyp
From Proteopedia
| Line 5: | Line 5: | ||
==Overview== | ==Overview== | ||
| - | Thermotoga maritima invertase (beta-fructosidase) hydrolyzes sucrose to, release fructose and glucose, which are major carbon and energy sources, for both prokaryotes and eukaryotes. The name "invertase" was given to, this enzyme over a century ago, because the 1:1 mixture of glucose and, fructose that it produces was named "invert sugar." Despite its name, the, enzyme operates with a mechanism leading to the retention of the anomeric, configuration at the site of cleavage. The enzyme belongs to family GH32, of the sequence-based classification of glycosidases. The crystal, structure, determined at 2-A resolution, reveals two modules, namely a, five-bladed beta-propeller with structural similarity to the, beta-propeller structures of glycosidase from families GH43 and GH68, connected to a ... | + | Thermotoga maritima invertase (beta-fructosidase) hydrolyzes sucrose to, release fructose and glucose, which are major carbon and energy sources, for both prokaryotes and eukaryotes. The name "invertase" was given to, this enzyme over a century ago, because the 1:1 mixture of glucose and, fructose that it produces was named "invert sugar." Despite its name, the, enzyme operates with a mechanism leading to the retention of the anomeric, configuration at the site of cleavage. The enzyme belongs to family GH32, of the sequence-based classification of glycosidases. The crystal, structure, determined at 2-A resolution, reveals two modules, namely a, five-bladed beta-propeller with structural similarity to the, beta-propeller structures of glycosidase from families GH43 and GH68, connected to a beta-sandwich module. Three carboxylates at the bottom of a, deep, negatively charged funnel-shaped depression of the beta-propeller, are essential for catalysis and function as nucleophile, general acid, and, transition state stabilizer, respectively. The catalytic machinery of, invertase is perfectly superimposable to that of the enzymes of families, GH43 and GH68. The variation in the position of the furanose ring at the, site of cleavage explains the different mechanisms evident in families, GH32 and GH68 (retaining) and GH43 (inverting) furanosidases. |
==About this Structure== | ==About this Structure== | ||
| - | 1UYP is a | + | 1UYP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with SO4, NA, CIT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1UTW. Active as [http://en.wikipedia.org/wiki/Beta-fructofuranosidase Beta-fructofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.26 3.2.1.26] Structure known Active Site: CAT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UYP OCA]. |
==Reference== | ==Reference== | ||
| Line 30: | Line 30: | ||
[[Category: sucrose degradation]] | [[Category: sucrose degradation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:42:38 2007'' |
Revision as of 11:37, 5 November 2007
|
THE THREE-DIMENSIONAL STRUCTURE OF BETA-FRUCTOSIDASE (INVERTASE) FROM THERMOTOGA MARITIMA
Overview
Thermotoga maritima invertase (beta-fructosidase) hydrolyzes sucrose to, release fructose and glucose, which are major carbon and energy sources, for both prokaryotes and eukaryotes. The name "invertase" was given to, this enzyme over a century ago, because the 1:1 mixture of glucose and, fructose that it produces was named "invert sugar." Despite its name, the, enzyme operates with a mechanism leading to the retention of the anomeric, configuration at the site of cleavage. The enzyme belongs to family GH32, of the sequence-based classification of glycosidases. The crystal, structure, determined at 2-A resolution, reveals two modules, namely a, five-bladed beta-propeller with structural similarity to the, beta-propeller structures of glycosidase from families GH43 and GH68, connected to a beta-sandwich module. Three carboxylates at the bottom of a, deep, negatively charged funnel-shaped depression of the beta-propeller, are essential for catalysis and function as nucleophile, general acid, and, transition state stabilizer, respectively. The catalytic machinery of, invertase is perfectly superimposable to that of the enzymes of families, GH43 and GH68. The variation in the position of the furanose ring at the, site of cleavage explains the different mechanisms evident in families, GH32 and GH68 (retaining) and GH43 (inverting) furanosidases.
About this Structure
1UYP is a Single protein structure of sequence from Thermotoga maritima with SO4, NA, CIT and GOL as ligands. This structure superseeds the now removed PDB entry 1UTW. Active as Beta-fructofuranosidase, with EC number 3.2.1.26 Structure known Active Site: CAT. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases., Alberto F, Bignon C, Sulzenbacher G, Henrissat B, Czjzek M, J Biol Chem. 2004 Apr 30;279(18):18903-10. Epub 2004 Feb 18. PMID:14973124
Page seeded by OCA on Mon Nov 5 13:42:38 2007
