4mb1
From Proteopedia
(Difference between revisions)
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===The Structure of MalL mutant enzyme G202P from Bacillus subtilus=== | ===The Structure of MalL mutant enzyme G202P from Bacillus subtilus=== | ||
{{ABSTRACT_PUBMED_24015933}} | {{ABSTRACT_PUBMED_24015933}} | ||
+ | |||
+ | ==Function== | ||
+ | [[http://www.uniprot.org/uniprot/O16G1_BACSU O16G1_BACSU]] Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose. | ||
==About this Structure== | ==About this Structure== | ||
- | [[4mb1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[4mb1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MB1 OCA]. |
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:024015933</ref><references group="xtra"/><references/> | <ref group="xtra">PMID:024015933</ref><references group="xtra"/><references/> | ||
- | [[Category: | + | [[Category: Bacsu]] |
[[Category: Oligo-1,6-glucosidase]] | [[Category: Oligo-1,6-glucosidase]] | ||
[[Category: Arcus, V L.]] | [[Category: Arcus, V L.]] |
Revision as of 08:40, 27 November 2013
Contents |
The Structure of MalL mutant enzyme G202P from Bacillus subtilus
Template:ABSTRACT PUBMED 24015933
Function
[O16G1_BACSU] Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose.
About this Structure
4mb1 is a 1 chain structure with sequence from Bacsu. Full crystallographic information is available from OCA.
Reference
- Hobbs JK, Jiao W, Easter AD, Parker EJ, Schipper LA, Arcus VL. Change in Heat Capacity for Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates. ACS Chem Biol. 2013 Sep 17. PMID:24015933 doi:10.1021/cb4005029