1ose
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Two different crystal forms of pig pancreatic alpha-amylase isoenzyme II, (PPAII), free and complexed to a carbohydrate inhibitor (acarbose), have, been compared together and to previously reported structures of PPAI. A, crystal form obtained at 4 degrees C, containing nearly 72% solvent, made, it possible to obtain a new complex with acarbose, different from a, previous one obtained at 20 degrees C [Qian, M., Buisson, G., Duee, E., Haser, H. & Payan, F. (1994) Biochemistry 33, 6284-6294]. In the present, form, six contiguous subsites of the enzyme active site are occupied by, the carbohydrate ligand; the structural data indicate that the binding, site is capable of holding more than the five glucose units of the scheme, proposed through kinetic studies. A monosaccharide ring bridging ... | + | Two different crystal forms of pig pancreatic alpha-amylase isoenzyme II, (PPAII), free and complexed to a carbohydrate inhibitor (acarbose), have, been compared together and to previously reported structures of PPAI. A, crystal form obtained at 4 degrees C, containing nearly 72% solvent, made, it possible to obtain a new complex with acarbose, different from a, previous one obtained at 20 degrees C [Qian, M., Buisson, G., Duee, E., Haser, H. & Payan, F. (1994) Biochemistry 33, 6284-6294]. In the present, form, six contiguous subsites of the enzyme active site are occupied by, the carbohydrate ligand; the structural data indicate that the binding, site is capable of holding more than the five glucose units of the scheme, proposed through kinetic studies. A monosaccharide ring bridging two, protein molecules related by the crystal packing is located on the, surface, at a distance of 2.0 nm from the reducing end of the inhibitor, ligand; the symmetry-related glucose ring in the crystal lattice is found, 1.5 nm away from the non-reducing end of the inhibitor ligand. |
==About this Structure== | ==About this Structure== | ||
| - | 1OSE is a | + | 1OSE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with GLC, CL and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Structure known Active Sites: AS1, AS2, AS3, AS4, AS5, CAL and CLO. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OSE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''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 14:14:18 2007'' |
Revision as of 12:08, 5 November 2007
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PORCINE PANCREATIC ALPHA-AMYLASE COMPLEXED WITH ACARBOSE
Overview
Two different crystal forms of pig pancreatic alpha-amylase isoenzyme II, (PPAII), free and complexed to a carbohydrate inhibitor (acarbose), have, been compared together and to previously reported structures of PPAI. A, crystal form obtained at 4 degrees C, containing nearly 72% solvent, made, it possible to obtain a new complex with acarbose, different from a, previous one obtained at 20 degrees C [Qian, M., Buisson, G., Duee, E., Haser, H. & Payan, F. (1994) Biochemistry 33, 6284-6294]. In the present, form, six contiguous subsites of the enzyme active site are occupied by, the carbohydrate ligand; the structural data indicate that the binding, site is capable of holding more than the five glucose units of the scheme, proposed through kinetic studies. A monosaccharide ring bridging two, protein molecules related by the crystal packing is located on the, surface, at a distance of 2.0 nm from the reducing end of the inhibitor, ligand; the symmetry-related glucose ring in the crystal lattice is found, 1.5 nm away from the non-reducing end of the inhibitor ligand.
About this Structure
1OSE is a Single protein structure of sequence from Sus scrofa with GLC, CL and CA as ligands. Active as Alpha-amylase, with EC number 3.2.1.1 Structure known Active Sites: AS1, AS2, AS3, AS4, AS5, CAL and CLO. Full crystallographic information is available from OCA.
Reference
Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose., Gilles C, Astier JP, Marchis-Mouren G, Cambillau C, Payan F, Eur J Biochem. 1996 Jun 1;238(2):561-9. PMID:8681972
Page seeded by OCA on Mon Nov 5 14:14:18 2007
Categories: Alpha-amylase | Single protein | Sus scrofa | Gilles, C. | Payan, F. | CA | CL | GLC | Acarbose | Hydrolase | Hydrolase (o-glycosyl)
