1gah
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1GAH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Aspergillus_awamori Aspergillus awamori]] with MAN, ACR, SER and GLY as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1GAH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Aspergillus_awamori Aspergillus awamori]] with MAN, ACR, SER and GLY as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Glucan_1,4-alpha-glucosidase Glucan 1,4-alpha-glucosidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.3 3.2.1.3]]. Structure known Active Sites: SB1, SB2 and SB3. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GAH OCA]]. |
==Reference== | ==Reference== | ||
Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism., Aleshin AE, Stoffer B, Firsov LM, Svensson B, Honzatko RB, Biochemistry. 1996 Jun 25;35(25):8319-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8679589 8679589] | Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism., Aleshin AE, Stoffer B, Firsov LM, Svensson B, Honzatko RB, Biochemistry. 1996 Jun 25;35(25):8319-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8679589 8679589] | ||
[[Category: Aspergillus awamori]] | [[Category: Aspergillus awamori]] | ||
| + | [[Category: Glucan 1,4-alpha-glucosidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aleshin, A.E.]] | [[Category: Aleshin, A.E.]] | ||
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[[Category: polysaccharide degradation]] | [[Category: polysaccharide degradation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:30:06 2007'' |
Revision as of 08:25, 30 October 2007
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GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE
Overview
Crystal structures at pH 4 of complexes of glucoamylase from Aspergillus, awamori var. X100 with the pseudotetrasaccharides D-gluco-dihydroacarbose, and acarbose have been refined to R-factors of 0.147 and 0.131 against, data to 1.7- and 2.0-A resolution, respectively. The two inhibitors bind, in nearly identical manners, each exhibiting a dual binding mode with, respect to the location of the last sugar residues. The reduced affinity, of D-gluco-dihydroacarbose (K1 = 10(-8) M) relative to acarbose (K1 =, 10(-12) M) may stem in part from the weakening of hydrogen bonds of the, catalytic water (Wat 500) to the enzyme. Steric contacts between the, nonreducing end of D-gluco-dihydroacarbose and the catalytic water perturb, Wat 500 from its site of optimal hydrogen bonding to the active ... [(full description)]
About this Structure
1GAH is a [Single protein] structure of sequence from [Aspergillus awamori] with MAN, ACR, SER and GLY as [ligands]. Active as [Glucan 1,4-alpha-glucosidase], with EC number [3.2.1.3]. Structure known Active Sites: SB1, SB2 and SB3. Full crystallographic information is available from [OCA].
Reference
Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism., Aleshin AE, Stoffer B, Firsov LM, Svensson B, Honzatko RB, Biochemistry. 1996 Jun 25;35(25):8319-28. PMID:8679589
Page seeded by OCA on Tue Oct 30 10:30:06 2007
