1E4M
 
 | | MYROSINASE FROM SINAPIS ALBA | | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... | | Authors: | Burmeister, W.P. | | Deposit date: | 2000-07-10 | | Release date: | 2001-05-25 | | Last modified: | 2024-10-23 | | Method: | X-RAY DIFFRACTION (1.2 Å) | | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base
J.Biol.Chem., 275, 2000
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1E72
 | | Myrosinase from Sinapis alba with bound gluco-hydroximolactam and sulfate or ascorbate | | Descriptor: | (2S,3S,4R,5R)-6-(HYDROXYAMINO)-2-(HYDROXYMETHYL)-2,3,4,5-TETRAHYDROPYRIDINE-3,4,5-TRIOL, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... | | Authors: | Burmeister, W.P. | | Deposit date: | 2000-08-23 | | Release date: | 2001-01-05 | | Last modified: | 2024-10-23 | | Method: | X-RAY DIFFRACTION (1.6 Å) | | Cite: | High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base.
J. Biol. Chem., 275, 2000
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1E70
 | | 2-F-glucosylated MYROSINASE FROM SINAPIS ALBA | | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-deoxy-2-fluoro-alpha-D-glucopyranose, ... | | Authors: | Burmeister, W.P. | | Deposit date: | 2000-08-23 | | Release date: | 2001-01-05 | | Last modified: | 2024-10-23 | | Method: | X-RAY DIFFRACTION (1.65 Å) | | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base
J.Biol.Chem., 275, 2000
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1E6Q
 | | MYROSINASE FROM SINAPIS ALBA with the bound transition state analogue gluco-tetrazole | | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... | | Authors: | Burmeister, W.P. | | Deposit date: | 2000-08-22 | | Release date: | 2001-01-05 | | Last modified: | 2024-10-23 | | Method: | X-RAY DIFFRACTION (1.35 Å) | | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base
J.Biol.Chem., 275, 2000
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1E71
 | | MYROSINASE FROM SINAPIS ALBA with bound ascorbate | | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ASCORBIC ACID, ... | | Authors: | Burmeister, W.P. | | Deposit date: | 2000-08-23 | | Release date: | 2001-01-05 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (1.5 Å) | | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base
J.Biol.Chem., 275, 2000
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1E73
 | | 2-F-glucosylated MYROSINASE FROM SINAPIS ALBA with bound L-ascorbate | | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-deoxy-2-fluoro-alpha-D-glucopyranose, ... | | Authors: | Burmeister, W.P. | | Deposit date: | 2000-08-23 | | Release date: | 2001-01-05 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (1.5 Å) | | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base
J.Biol.Chem., 275, 2000
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1E6S
 | | MYROSINASE FROM SINAPIS ALBA with bound gluco-hydroximolactam and sulfate | | Descriptor: | (2S,3S,4R,5R)-6-(HYDROXYAMINO)-2-(HYDROXYMETHYL)-2,3,4,5-TETRAHYDROPYRIDINE-3,4,5-TRIOL, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... | | Authors: | Burmeister, W.P. | | Deposit date: | 2000-08-23 | | Release date: | 2000-09-06 | | Last modified: | 2024-11-13 | | Method: | X-RAY DIFFRACTION (1.35 Å) | | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base
J.Biol.Chem., 275, 2000
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1E6X
 | | MYROSINASE FROM SINAPIS ALBA with a bound transition state analogue,D-glucono-1,5-lactone | | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, D-glucono-1,5-lactone, ... | | Authors: | Burmeister, W.P. | | Deposit date: | 2000-08-23 | | Release date: | 2001-01-05 | | Last modified: | 2024-10-23 | | Method: | X-RAY DIFFRACTION (1.6 Å) | | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base
J.Biol.Chem., 275, 2000
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1W9B
 | | S. alba myrosinase in complex with carba-glucotropaeolin | | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CARBA-GLUCOTROPAEOLIN, ... | | Authors: | Bourderioux, A, Lefoix, M, Gueyrard, D, Tatibouet, A, Cottaz, S, Arzt, S, Burmeister, W.P, Rollin, P. | | Deposit date: | 2004-10-08 | | Release date: | 2005-05-19 | | Last modified: | 2024-10-16 | | Method: | X-RAY DIFFRACTION (1.7 Å) | | Cite: | The glucosinolate-myrosinase system. New insights into enzyme-substrate interactions by use of simplified inhibitors.
Org. Biomol. Chem., 3, 2005
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1W9D
 | | S. alba myrosinase in complex with S-ethyl phenylacetothiohydroximate- O-sulfate | | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... | | Authors: | Bourderioux, A, Lefoix, M, Gueyrard, D, Tatibouet, A, Cottaz, S, Arzt, S, Burmeister, W.P, Rollin, P. | | Deposit date: | 2004-10-08 | | Release date: | 2005-05-19 | | Last modified: | 2024-10-23 | | Method: | X-RAY DIFFRACTION (1.6 Å) | | Cite: | The Glucosinolate-Myrosinase System. New Insights Into Enzyme-Substrate Interactions by Use of Simplified Inhibitors
Org.Biomol.Chem., 3, 2005
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