Alpha-glucosidase
From Proteopedia
(Difference between revisions)
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</StructureSection> | </StructureSection> | ||
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- | ==3D structures of α-glucosidase== | ||
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- | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
- | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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- | *α glucosidase | ||
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- | **[[2g3m]] – SsAGS – ''Sulfolobus solfataricus''<br /> | ||
- | **[[2ze0]], [[5zcb]] – GeAGS – ''Geobacillus''<br /> | ||
- | **[[3w38]] – bAGS - beet<br /> | ||
- | **[[2d73]], [[2jka]], [[3wfa]], [[5djw]], [[5f7c]], [[3wfa]], [[3a24]], [[5xfm]] – BtAGS – ''Bacterioides thetaiotaomicron''<br /> | ||
- | **[[5hq4]] – PaAGS - ''Pseudoalteromonas''<br /> | ||
- | **[[1lf6]] – TtAGS – ''Thermoanaerobobacterium thermosaccharolyticum''<br /> | ||
- | **[[1kum]], [[1kul]] – AnAGS starch-binding domain – ''Aspergillus niger'' - NMR<br /> | ||
- | **[[3eqa]] – AnAGS catalytic domain <br /> | ||
- | **[[1glm]], [[3gly]] – AaAGS – ''Aspergillus awamori''<br /> | ||
- | **[[1ayx]], [[2fba]] – SfAGS – ''Saccharomycopsis fibuligera''<br /> | ||
- | **[[5f0e]] – mAGS - mouse<br /> | ||
- | **[[5aed]], [[5aee]], [[5aeg]] – AGS - ''Esherichia coli''<br /> | ||
- | **[[3wy1]] – HaAGS - ''Halomonas''<br /> | ||
- | **[[4xpo]] – PsAGS - ''Pedobacter saltans''<br /> | ||
- | **[[4xpr]] – PsAGS (mutant)<br /> | ||
- | **[[2lvx]] – fyAGS 2 MRH domain – fission yeast - NMR<br /> | ||
- | **[[2n1h]] – fyAGS 2 MRH domain (mutant) - NMR<br /> | ||
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- | *α-glucosidase complex | ||
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- | **[[2jke]] – BtAGS + deoxynojirimycin<br /> | ||
- | **[[2jkp]] – BtAGS + castasnospermine<br /> | ||
- | **[[2zq0]] – BtAGS + acarbose<br /> | ||
- | **[[5hqa]] – PaAGS + acarbose <br /> | ||
- | **[[5hqb]] – PaAGS (mutant) + panose <br /> | ||
- | **[[1lf9]] – TtAGS + acarbose<br /> | ||
- | **[[1gai]], [[1gah]], [[1agm]] – AaAGS + acarbose<br /> | ||
- | **[[2f6d]] – SfAGS + acarbose<br /> | ||
- | **[[1dog]] – AaAGS + deoxynojirimycin<br /> | ||
- | **[[1acz]], [[1ac0]] – AGS starch-binding domain + cyclodextrin - NMR<br /> | ||
- | **[[5hjr]] – AGS + glucosidase subunit beta - mouse<br /> | ||
- | **[[5h9o]] – mAGS + glucose<br /> | ||
- | **[[5hjo]] – mAGS + substrate analog<br /> | ||
- | **[[5h9r]] – mAGS + intermediate<br /> | ||
- | **[[5ied]], [[5iee]], [[5ief]], [[5ieg]] – mAGS + iminosugar antiviral<br /> | ||
- | **[[3wy2]] – HaAGS + glucose<br /> | ||
- | **[[3wy3]] – HaAGS (mutant) + glucose<br /> | ||
- | **[[3wy4]] – HaAGS (mutant) + maltose<br /> | ||
- | **[[4xpp]] – PsAGS + galactose<br /> | ||
- | **[[4xpq]] – PsAGS + fucose<br /> | ||
- | **[[4xps]] – PsAGS (mutant) + galactpiranoside<br /> | ||
- | **[[3wel]], [[3wem]], [[3wen]], [[3weo]], [[3w37]] – bAGS + substrate<br /> | ||
- | **[[4xqm]] – fyAGS 2 MRH domain + mannose<br /> | ||
- | **[[5zcc]] – GeAGS (mutant) + maltose<br /> | ||
- | **[[5zcd]] – GeAGS (mutant) + maltotriose<br /> | ||
- | **[[5zce]] – GeAGS (mutant) + maltotetraose<br /> | ||
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- | *Alpha-glucosidase YIHQ | ||
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- | **[[5ohs]] – RrYIHQ + sulfoquinovoside derivative – ''Rhizobium radiobacter''<br /> | ||
- | **[[5ohy]] – RrYIHQ + inhibitor<br /> | ||
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- | *Maltase | ||
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- | **[[1vjt]] – TmAGS + NAD – ''Thermotoga maritima''<br /> | ||
- | **[[1obb]] – TmAGS + NAD + maltose <br /> | ||
- | **[[2g3n]] – SsAGS + octylglucoside<br /> | ||
- | **[[3ton]], [[5kzw]], [[5kzx]], [[5nn3]], [[5nn4]] – hAGS C-terminal - human<br /> | ||
- | **[[5nn8]] – hAGS + acarbose <br /> | ||
- | **[[3top]] – hAGS C-terminal + acarbose <br /> | ||
- | **[[3l4y]], [[3l4z]], [[3l4x]], [[3l4w]], [[3l4v]], [[3l4u]], [[3l4t]] – hAGS N-terminal + inhibitor<br /> | ||
- | **[[5nn5]], [[5nn6]] – hAGS + jiromycin derivative<br /> | ||
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- | *Maltase-glucoamylase | ||
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- | **[[2qly]] – hAGS N-terminal catalytic subunit<br /> | ||
- | **[[2qmj]] – hAGS N-terminal catalytic subunit + acarbose<br /> | ||
- | **[[3ctt]] – hAGS N-terminal catalytic subunit + casuarine<br /> | ||
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- | *Isomaltase or oligo-1,6-glucosidase | ||
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- | **[[3a47]], [[3aj7]] – yAGS – yeast<br /> | ||
- | **[[3a4a]], [[3axh]] – yAGS + glucose<br /> | ||
- | **[[3axi]] – yAGS (mutant) + glucose<br /> | ||
- | **[[3n04]] – RoAGS – ''Ruminococcus obeum''<br /> | ||
- | **[[3nsx]], [[3nuk]] – RoAGS (mutant)<br /> | ||
- | **[[3pha]], [[3poc]] – RoAGS (mutant) + acarbose<br /> | ||
- | **[[3mkk]] – RoAGS + isomaltose <br /> | ||
- | **[[4m8u]], [[4maz]], [[4mb1]] – BsAGS 1 (mutant) – ''Bacillus subtilis''<br /> | ||
- | **[[4m56]] – BsAGS 1 + glucose <br /> | ||
- | **[[5wcz]] – BsAGS 1 + deoxynojirimycin analog<br /> | ||
- | **[[1uok]] – AGS – Bacillus cereus<br /> | ||
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- | *Sucrase–isomaltase | ||
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- | **[[3lpo]] – hAGS N-terminal <br /> | ||
- | **[[3lpp]] – hAGS N-terminal + kotalanol<br /> | ||
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- | *Maltodextrin glucosidase | ||
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- | **[[5bn7]] – EcAGS <br /> | ||
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- | *6-phospho-α-glucosidase | ||
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- | **[[1u8x]] – BsPAGS + α-glucose phosphate + NAD <br /> | ||
- | **[[6dux]] – KpPAGS + malate + NAD – ''Klebsiella pneumoniae''<br /> | ||
- | **[[6dvv]] – KpPAGS + Mn + NAD <br /> | ||
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- | *Glucan 1,4-alpha glucosidase or glucoamylase | ||
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- | **[[6frv]] – AnGAGS catalytic domain residues 25-640<br /> | ||
- | **[[5ghl]] – AnGAGS starch-binding domain residues 533-640<br /> | ||
- | **[[6fhv]] – GAGS – Penicillium oxalicum<br /> | ||
- | **[[6fhw]] – GAGS – Amorphotheca resinae<br /> | ||
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- | *Glucan 1,6-α-glucosidase or dextran glucosidase | ||
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- | **[[4aie]] – GAGS – ''Lactobacillus acidophilus''<br /> | ||
- | **[[2zic]], [[4xb3]] – SmGAGS (mutant) – ''Streptococcus mutans''<br /> | ||
- | **[[4wlc]] – SmGAGS + glucose <br /> | ||
- | **[[2zid]] – SmGAGS (mutant) + isomaltotriose<br /> | ||
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- | }} | ||
== References == | == References == |
Revision as of 08:21, 6 March 2019
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References
- ↑ Gloster TM, Turkenburg JP, Potts JR, Henrissat B, Davies GJ. Divergence of catalytic mechanism within a glycosidase family provides insight into evolution of carbohydrate metabolism by human gut flora. Chem Biol. 2008 Oct 20;15(10):1058-67. Epub 2008 Oct 9. PMID:18848471 doi:10.1016/j.chembiol.2008.09.005
- ↑ Yamamoto K, Miyake H, Kusunoki M, Osaki S. Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose. FEBS J. 2010 Oct;277(20):4205-14. doi: 10.1111/j.1742-4658.2010.07810.x., Epub 2010 Aug 31. PMID:20812985 doi:10.1111/j.1742-4658.2010.07810.x