The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution
about
Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastorisCrystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitorThe structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymesOptimization to low temperature activity in psychrophilic enzymesThe cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolutionCrystal structures of human pancreatic alpha-amylase in complex with carbohydrate and proteinaceous inhibitorsThree camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topologyStructural basis of α-amylase activation by chlorideThe fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activityCrystal Structure of Bacillus subtilis -Amylase in Complex with AcarboseX-ray Crystallographic Analyses of Pig Pancreatic α-Amylase with Limit Dextrin, Oligosaccharide, and α-Cyclodextrin ,Metal-Dependent Conformational Activation Explains Highly Promutagenic Replication across O6-Methylguanine by Human DNA Polymerase βStructural characterization of the ribonuclease H-like type ASKHA superfamily kinase MK0840 from Methanopyrus kandleriCrystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and productsEngineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1Trehalose synthase converts glycogen to trehaloseThe crystal structure of the processive endocellulase CelF of Clostridium cellulolyticum in complex with a thiooligosaccharide inhibitor at 2.0 A resolution.A circularly permuted alpha-amylase-type alpha/beta-barrel structure in glucan-synthesizing glucosyltransferases.Molecular basis of cold adaptation.Alpha-amylase inhibitors selected from a combinatorial library of a cellulose binding domain scaffold.Cloning, sequencing, and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme.Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic α-amylase from Antarctic Bacterium.Cloning and expression analysis of the Bombyx mori α-amylase gene (Amy) from the indigenous Thai silkworm strain, Nanglai.Epigallocatechin gallate affects glucose metabolism and increases fitness and lifespan in Drosophila melanogasterImplication for buried polar contacts and ion pairs in hyperthermostable enzymes.Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial bindingPsychrophilic enzymes: from folding to function and biotechnology.α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass.Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and -5/-6 of barley alpha-amylase 1.Carbohydrate binding sites in a pancreatic alpha-amylase-substrate complex, derived from X-ray structure analysis at 2.1 A resolutionEnzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase.Oral Fusobacterium nucleatum subsp. polymorphum binds to human salivary α-amylase.Mechanism of porcine pancreatic alpha-amylase inhibition of amylose and maltopentaose hydrolysis by kidney bean (Phaseolus vulgaris) inhibitor and comparison with that by acarbose.Oligosaccharide binding to barley alpha-amylase 1.Acarbose, a pseudooligosaccharide, is transported but not metabolized by the maltose-maltodextrin system of Escherichia coli.In situ extension as an approach for identifying novel alpha-amylase inhibitors.Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03 A resolutionImproved activity and modulated action pattern obtained by random mutagenesis at the fourth beta-alpha loop involved in substrate binding to the catalytic (beta/alpha)8-barrel domain of barley alpha-amylase 1.Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley alpha-amylase 1.
P2860
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P2860
The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution
description
1994 nî lūn-bûn
@nan
1994 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
The active center of a mammali ...... or refined to 2.2-A resolution
@ast
The active center of a mammali ...... or refined to 2.2-A resolution
@en
The active center of a mammali ...... or refined to 2.2-A resolution
@nl
type
label
The active center of a mammali ...... or refined to 2.2-A resolution
@ast
The active center of a mammali ...... or refined to 2.2-A resolution
@en
The active center of a mammali ...... or refined to 2.2-A resolution
@nl
prefLabel
The active center of a mammali ...... or refined to 2.2-A resolution
@ast
The active center of a mammali ...... or refined to 2.2-A resolution
@en
The active center of a mammali ...... or refined to 2.2-A resolution
@nl
P2093
P356
P1433
P1476
The active center of a mammali ...... or refined to 2.2-A resolution
@en
P2093
P304
P356
10.1021/BI00186A031
P407
P577
1994-05-24T00:00:00Z