1ob0
KINETIC STABILIZATION OF BACILLUS LICHENIFORMIS-AMYLASE THROUGH INTRODUCTION OF HYDROPHOBIC RESIDUES AT THE SURFACEKINETIC STABILIZATION OF BACILLUS LICHENIFORMIS-AMYLASE THROUGH INTRODUCTION OF HYDROPHOBIC RESIDUES AT THE SURFACE
Template:ABSTRACT PUBMED 12540849
About this StructureAbout this Structure
1ob0 is a 1 chain structure of Alpha-Amylase with sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.
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ReferenceReference
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- ↑ Machius M, Declerck N, Huber R, Wiegand G. Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface. J Biol Chem. 2003 Mar 28;278(13):11546-53. Epub 2003 Jan 21. PMID:12540849 doi:10.1074/jbc.M212618200
- ↑ Hwang KY, Song HK, Chang C, Lee J, Lee SY, Kim KK, Choe S, Sweet RM, Suh SW. Crystal structure of thermostable alpha-amylase from Bacillus licheniformis refined at 1.7 A resolution. Mol Cells. 1997 Apr 30;7(2):251-8. PMID:9163741
- ↑ Machius M, Declerck N, Huber R, Wiegand G. Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure. 1998 Mar 15;6(3):281-92. PMID:9551551
- ↑ Machius M, Wiegand G, Huber R. Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution. J Mol Biol. 1995 Mar 3;246(4):545-59. PMID:7877175 doi:http://dx.doi.org/10.1006/jmbi.1994.0106