1ogo
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in, dextran polymers. The structure of dextranase, Dex49A, from Penicillium, minioluteum was solved in the apo-enzyme and product-bound forms. The main, domain of the enzyme is a right-handed parallel beta helix, which is, connected to a beta sandwich domain at the N terminus. In the structure of, the product complex, isomaltose was found to bind in a crevice on the, surface of the enzyme. The glycosidic oxygen of the glucose unit in, subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395., By NMR spectroscopy the reaction course was shown to occur with net, inversion at the anomeric carbon, implying a single displacement, mechanism. Both Asp376 and Asp396 are suitably positioned to activate the, .. | + | Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in, dextran polymers. The structure of dextranase, Dex49A, from Penicillium, minioluteum was solved in the apo-enzyme and product-bound forms. The main, domain of the enzyme is a right-handed parallel beta helix, which is, connected to a beta sandwich domain at the N terminus. In the structure of, the product complex, isomaltose was found to bind in a crevice on the, surface of the enzyme. The glycosidic oxygen of the glucose unit in, subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395., By NMR spectroscopy the reaction course was shown to occur with net, inversion at the anomeric carbon, implying a single displacement, mechanism. Both Asp376 and Asp396 are suitably positioned to activate the, water molecule that performs the nucleophilic attack. A new clan that, links glycoside hydrolase families 28 and 49 is suggested. |
==About this Structure== | ==About this Structure== | ||
| - | 1OGO is a | + | 1OGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_minioluteum Penicillium minioluteum]. Active as [http://en.wikipedia.org/wiki/Dextranase Dextranase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.11 3.2.1.11] Structure known Active Site: CAT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OGO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 15:04:21 2007'' |
Revision as of 12:59, 5 November 2007
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DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE
Overview
Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in, dextran polymers. The structure of dextranase, Dex49A, from Penicillium, minioluteum was solved in the apo-enzyme and product-bound forms. The main, domain of the enzyme is a right-handed parallel beta helix, which is, connected to a beta sandwich domain at the N terminus. In the structure of, the product complex, isomaltose was found to bind in a crevice on the, surface of the enzyme. The glycosidic oxygen of the glucose unit in, subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395., By NMR spectroscopy the reaction course was shown to occur with net, inversion at the anomeric carbon, implying a single displacement, mechanism. Both Asp376 and Asp396 are suitably positioned to activate the, water molecule that performs the nucleophilic attack. A new clan that, links glycoside hydrolase families 28 and 49 is suggested.
About this Structure
1OGO is a Single protein structure of sequence from Penicillium minioluteum. Active as Dextranase, with EC number 3.2.1.11 Structure known Active Site: CAT. Full crystallographic information is available from OCA.
Reference
Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex., Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA, Structure. 2003 Sep;11(9):1111-21. PMID:12962629
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