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| | {{STRUCTURE_1sma| PDB=1sma | SCENE= }} | | {{STRUCTURE_1sma| PDB=1sma | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF A MALTOGENIC AMYLASE'''
| + | ===CRYSTAL STRUCTURE OF A MALTOGENIC AMYLASE=== |
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| - | ==Overview==
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| - | Amylases catalyze the hydrolysis of starch material and play central roles in carbohydrate metabolism. Compared with many different amylases that are able to hydrolyze only alpha-D-(1,4)-glycosidic bonds, maltogenic amylases exhibit catalytic versatility: hydrolysis of alpha-D-(1,4)- and alpha-D-(1,6)-glycosidic bonds and transglycosylation of oligosaccharides to C3-, C4-, or C6-hydroxyl groups of various acceptor mono- or disaccharides. It has been speculated that the catalytic property of the enzymes is linked to the additional approximately 130 residues at the N terminus that are absent in other typical alpha-amylases. The crystal structure of a maltogenic amylase from a Thermus strain was determined at 2.8 A. The structure, an analytical centrifugation, and a size exclusion column chromatography proved that the enzyme is a dimer in solution. The N-terminal segment of the enzyme folds into a distinct domain and comprises the enzyme active site together with the central (alpha/beta)(8) barrel of the adjacent subunit. The active site is a narrow and deep cleft suitable for binding cyclodextrins, which are the preferred substrates to other starch materials. At the bottom of the active site cleft, an extra space, absent in the other typical alpha-amylases, is present whose size is comparable with that of a disaccharide. The space is most likely to host an acceptor molecule for the transglycosylation and to allow binding of a branched oligosaccharide for hydrolysis of alpha-D-(1,4)-glycosidic or alpha-D-(1,6)-glycosidic bond. The (alpha/beta)(8) barrel of the enzyme is the preserved scaffold in all the known amylases. The structure represents a novel example of how an enzyme acquires a different substrate profile and a catalytic versatility from a common active site and represents a framework for explaining the catalytic activities of transglycosylation and hydrolysis of alpha-D-(1,6)-glycosidic bond.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10473583}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10473583 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10473583}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Transglycosylation]] | | [[Category: Transglycosylation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:52:48 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:54:49 2008'' |
Revision as of 23:54, 28 July 2008
Template:STRUCTURE 1sma
CRYSTAL STRUCTURE OF A MALTOGENIC AMYLASE
Template:ABSTRACT PUBMED 10473583
About this Structure
1SMA is a Single protein structure of sequence from Thermus sp. im6501. Full crystallographic information is available from OCA.
Reference
Crystal structure of a maltogenic amylase provides insights into a catalytic versatility., Kim JS, Cha SS, Kim HJ, Kim TJ, Ha NC, Oh ST, Cho HS, Cho MJ, Kim MJ, Lee HS, Kim JW, Choi KY, Park KH, Oh BH, J Biol Chem. 1999 Sep 10;274(37):26279-86. PMID:10473583
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