This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Alpha-glucosidase
From Proteopedia
(Difference between revisions)
| Line 20: | Line 20: | ||
{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | * | + | *α glucosidase |
**[[2g3m]] – SsAGS – ''Sulfolobus solfataricus''<br /> | **[[2g3m]] – SsAGS – ''Sulfolobus solfataricus''<br /> | ||
**[[2ze0]] – AGS – ''Geobacillus''<br /> | **[[2ze0]] – AGS – ''Geobacillus''<br /> | ||
**[[3w38]] – bAGS - beet<br /> | **[[3w38]] – bAGS - beet<br /> | ||
| - | **[[2d73]], [[2jka]], [[3wfa]], [[5djw]], [[5f7c]], [[3wfa]], [[3a24]] – BtAGS – ''Bacterioides thetaiotaomicron''<br /> | + | **[[2d73]], [[2jka]], [[3wfa]], [[5djw]], [[5f7c]], [[3wfa]], [[3a24]], [[5xfm]] – BtAGS – ''Bacterioides thetaiotaomicron''<br /> |
**[[5hq4]] – PaAGS - ''Pseudoalteromonas''<br /> | **[[5hq4]] – PaAGS - ''Pseudoalteromonas''<br /> | ||
**[[1lf6]] – TtAGS – ''Thermoanaerobobacterium thermosaccharolyticum''<br /> | **[[1lf6]] – TtAGS – ''Thermoanaerobobacterium thermosaccharolyticum''<br /> | ||
| Line 37: | Line 37: | ||
**[[4xpo]] – PsAGS - ''Pedobacter saltans''<br /> | **[[4xpo]] – PsAGS - ''Pedobacter saltans''<br /> | ||
**[[4xpr]] – PsAGS (mutant)<br /> | **[[4xpr]] – PsAGS (mutant)<br /> | ||
| + | **[[2lvx]] – fyAGS 2 MRH domain – fission yeast - NMR<br /> | ||
| + | **[[2n1h]] – fyAGS 2 MRH domain (mutant) - NMR<br /> | ||
| - | * | + | *α-glucosidase complex |
**[[2jke]] – BtAGS + deoxynojirimycin<br /> | **[[2jke]] – BtAGS + deoxynojirimycin<br /> | ||
| Line 62: | Line 64: | ||
**[[4xps]] – PsAGS (mutant) + galactpiranoside<br /> | **[[4xps]] – PsAGS (mutant) + galactpiranoside<br /> | ||
**[[3wel]], [[3wem]], [[3wen]], [[3weo]], [[3w37]] – bAGS + substrate<br /> | **[[3wel]], [[3wem]], [[3wen]], [[3weo]], [[3w37]] – bAGS + substrate<br /> | ||
| + | **[[4xqm]] – fyAGS 2 MRH domain + mannose<br /> | ||
| - | *Maltase | + | *Maltase |
**[[1vjt]] – TmAGS + NAD – ''Thermotoga maritima''<br /> | **[[1vjt]] – TmAGS + NAD – ''Thermotoga maritima''<br /> | ||
**[[1obb]] – TmAGS + NAD + maltose <br /> | **[[1obb]] – TmAGS + NAD + maltose <br /> | ||
**[[2g3n]] – SsAGS + octylglucoside<br /> | **[[2g3n]] – SsAGS + octylglucoside<br /> | ||
| - | **[[3ton]] – hAGS C-terminal - human<br /> | + | **[[3ton]], [[5kzw]], [[5kzx]], [[5nn3]], [[5nn4]] – hAGS C-terminal - human<br /> |
| + | **[[5nn8]] – hAGS + acarbose <br /> | ||
**[[3top]] – hAGS C-terminal + acarbose <br /> | **[[3top]] – hAGS C-terminal + acarbose <br /> | ||
**[[3l4y]], [[3l4z]], [[3l4x]], [[3l4w]], [[3l4v]], [[3l4u]], [[3l4t]] – hAGS N-terminal + inhibitor<br /> | **[[3l4y]], [[3l4z]], [[3l4x]], [[3l4w]], [[3l4v]], [[3l4u]], [[3l4t]] – hAGS N-terminal + inhibitor<br /> | ||
| + | **[[5nn5]], [[5nn6]] – hAGS + jiromycin derivative<br /> | ||
*Isomaltase | *Isomaltase | ||
| Line 85: | Line 90: | ||
**[[5bn7]] – EcAGS <br /> | **[[5bn7]] – EcAGS <br /> | ||
| + | |||
| + | *6-phospho-α-glucosidase | ||
| + | |||
| + | **[[1u8x]] – PAGS + α-glucose phosphate + NAD – ''Bacillus subtilis''<br /> | ||
| + | |||
| + | *Glucan 1,6-α-glucosidase (dextran glucosidase) | ||
| + | |||
| + | **[[4aie]] – GAGS – ''Lactobacillus acidophilus''<br /> | ||
| + | **[[2zic]], [[4xb3]] – SmGAGS (mutant) – ''Streptococcus mutans''<br /> | ||
| + | **[[4wlc]] – SmGAGS + glucose <br /> | ||
| + | **[[2zid]] – SmGAGS (mutant) + isomaltotriose<br /> | ||
| + | |||
Revision as of 08:06, 12 March 2018
| |||||||||||
3D structures of α-glucosidase
Updated on 12-March-2018
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
