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3.2.1.1: alpha-amylase

This is an abbreviated version!
For detailed information about alpha-amylase, go to the full flat file.

Word Map on EC 3.2.1.1

Reaction

(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose
+
H2O
=
(alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose
 +
(alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose

Synonyms

1,4-alpha-D-glucan glucanohydrolase, 1,4-alpha-D-glucan glucanohydrolase and endoamylase, 1,4-alpha-D-glucan-glucanohydrolase, ABA, acid-stable amylase, acidic amylase, AGXA, AHA, alkaline alpha-amylase, alkalophilic Bacillus alpha-amylase, alpha amylase, alpha amylase 1, alpha-(1,4)-D-glucan glucanohydrolase, alpha-1,4 glucan-glucanohydrolase, alpha-1,4-glucan-4-glucanohydrolase, alpha-1-4 D-glucan glucanohydrolase, alpha-amylase, alpha-amylase 1, alpha-amylase 2, alpha-amylase 3, alpha-amylase A4, alpha-amylase Aasp, alpha-amylase AI, alpha-amylase AOA, Alpha-amylase carcinoid, alpha-amylase CMA, alpha-amylase gt, alpha-amylase HA, alpha-amylase I, alpha-amylase II, alpha-amylase PA, alpha-amylase PPA, alpha-amylase type A isozyme, alpha-amylase type II, alpha-amylase ZSA, alpha-amylases 1, AMF-3, ami, Amy, Amy B, Amy c6, Amy I, Amy II, Amy-1E, amy-CS2, Amy-E, Amy-FC1, AMY1, AMY121, AMY2, Amy3, amy5, Amy7C, AmyA, AmyB, AmyC, AmyCR, AmyD, AmyD-1, AmyE, AmyH, AmyI-1, AmyI3C6, AmyK, AmyK38, AmyL, Amyl III, amylase AI, amylase AII, amylase I, Amylase THC 250, amylase, alpha-, Amylopsin, amylopullulanase, AmyN26, AmyP, AmyQ, AmyS, AmyUS100, AmyUS100DELTAIG, AmyZ2, AOA, AoA1, AoA2, ApkA, Apu, B4168_3135, Ba-amy, BAA, Bacillus licheniformis alpha-amylase, Bactosol TK, barley alpha-amylase 1, BBG7_0117, BGTG-1, BH072alpha-amylase, BHA, BiLA, BLA, Blamy-I, bllj_0710, BMA.2, BSA-2, Bsamy-I, BSTA, Buclamase, Ca2+-independent alpha-amylase gt, CcAmy, CCAP, Clarase, Clone 103, Clone 168, Clone PHV19, Clones GRAMY56 and 963, cold-active alpha-amylase, cold-adapted alpha-amylase, ComA, crustacean cardioactive peptide, diastase, endo-1,4-alpha-D-glucan glucanohydrolase, endo-1,4-alpha-D-glucan glucohydrolase, endo-1,4-alpha-D-glucanohydrolase, endoamylase, FORILASE NTL alpha-amylase, Fortizyme, Fungamyl 800 L, G 995, G6-amylase, GH13Amy-1, GH13Amy-2, glycogenase, Gt-amy, HaAmy1, HaAmy2, haloalkaline alpha-amylase, HAS, HdAmyI, High pI alpha-amylase, HPA, HSA, HSAmy, HSAmy-ar, htur2110, human salivary alpha-amylase, hyperthermophilic alpha-amylase, Isozyme 1B, Kleistase L 1, KRA, LAMY, liquozyme, LLF-alpha-amylase, Low pI alpha-amylase, MalA, maltogenic amylase, maltohexaose-producing alpha-amylase, maltotriose-producing alpha-amylase, MAmy, Maxamyl, Maxilase, Meiotic expression upregulated protein 30, MJA1, More, N8 alpha-amylase, neutral amylase, Pancreatic alpha-amylase, PFTA, Pivozin, PPA, PPA-I, PPA-II, psychrophilic alpha amylase, Ptyalin, raw-starch-digesting alpha-amylase, RB5AMG_01539, Rbamy5, RBLA, RBSA-1, ROAmy, Ruminococcus bromii intermediary alpha-amylase 5, Saci_1162, salt-tolerant alpha-amylase, ScAmy43, Sfamy, Spitase CP 1, SSO1172, SusG, TAA, TaAmy3, Taka-amylase A, Takatherm, TcAmy, TdAmyA, tergal gland protein-1, TfAmy48, Thermamyl, Thermolase, thermostable alpha-amylase, TO_amyl, Tp-AmyS, TVA II, VAAmy1, VAAmy2, VrAmy, ZSA

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.1 alpha-amylase

Crystallization

Crystallization on EC 3.2.1.1 - alpha-amylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion technique at 23°C. Monoclinic crystal (space group P2(1)) form of alpha-amylase in complex with maltose at 1.8 A resolution. A 1.6 A resolution orthorhombic crystal form (space group P2(1)2(1)2) of the native enzyme is presented. Four maltose molecules are observed in the maltose-alpha-amylase complex
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purified modified enzyme TAAMOD, vapour diffusion, 10 mg/ml protein in 10 mM Tris, pH 7.5, and 5 mM CaCl2 against a solution of 20% PEG 4000, 0.4 M ammonium sulfate and 0.1 M MES, pH 7.2, 2 weeks, X-ray diffraction structure determination and analysis at 2.4 A reolution
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hanging drop vapor diffusion method, using 24% (w/v) PEG 3350 and 3.5 mM CaCl2 in 10 mM Tris buffer pH 7.5
hanging-drop vapor-diffusion method, crystal structure is determined at 2.1 A resolution
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recombinant enzyme
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SusG D498N mutant with bound maltoheptaose, Ca2+ replaces the Mg2+ ion observed in the apo structure, X-ray diffraction structure determination and analysis at 2.3 A resolution
tiny needle crystals are formed in 35 mM Na-acetate, pH 4.6, 35 mM CaCl2, 6.25% 2-propanol in the presence of 1.23% of the pseudo-oligosaccharide inhibitor acarbose at a protein concentration of 10 mg/ml, crystals diffract to 2.0 A resolution
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the circular dichroism spectrocopic data reveal the native alpha-amylase gt to contain 25% alpha-helix, 21% beta-sheet, and 54% random coils at pH 8.0. The fluorescence intensity increases with a shift in pH from neutral to acidic range while it decreases with increasing pH. With the pH change from neutral to basic, there is no significant change in the alpha-helix content. As the temperature increases from 40 to 110°C, no change in the alpha-helix content is observed, which remains around 22% at all temperatures
-
AmyA, X-ray diffraction structure determination and analysis at 1.6 A resolution
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two complexes of AmyB with carbohydrate ligands: the 1.35-A-resolution structure with the acarbose transglycosylation product, and the 2.2-A-resolution conplex of AmyB with alpha-cyclodextrin and hydrolysis products of maltoheptaose. The AmyB-acarbose complex includes residues 15-599, 1 acarbose molecule, 1 acarbose derived nonsaccharide, 2 glucose molecules, 4 calcium ions, 1 sodium ion, and 576 water molecules. The AmyB-maltoheptaose/cyclodextrin complex includes residues 14-599, 2 maltotetraose molecules, 1 alpha-cyclodextrin molecule, 7 calcium ions, 1 sodium ion, and 260 water molecules. The active site in AMyB is located at the C-terminal end of TIM barrel, with the residues Asp350, Glu380, and Asp447 as the catalytic residues
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crystals of wild-type and F256W mutant alpha-amylase, crystals diffract to 2.1 a resolution
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enzyme from salivary gland
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enzyme in complex with carbohydrate and proteinaceous inhibitors
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HSAmy and HSAmy-ar both show characteristics of a protein with ordered secondary structures, suggesting that the overall conformation of HSamy still retains in the mutant HSAmy-ar. Single or double mutations also do not alter the overall conformation of the enzyme
P04745
purified dimeric enzyme, hanging drop vapour diffusion method, 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is mixed with 0.001 ml of precipitation solution, three different successful variations, overview, 1 week, X-ray diffraction structure determination and analysis at 3.0 A resolution
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purified recombinant wild-type pancreatic enzyme, in complex with inhibitors acarbose, isoacarbose, or acarviosine-glucose, hanging drop vapour diffusion method, 0.005 ml of protein solution containing 16.3 mg/ml protein is mixed with 0.005 ml of reservoir solution containing 60% 2-methyl-2,4-pentanediol and 100 mM cacodylate, pH 7.5, 1 month, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution
recombinant wild-type and N298S variant HPAs are crystallized using the hanging drop vapor diffusion method
mutants Y105A/Y380A and H395A are crystallized
the structures of AMY1 Y380A and S378P are compared with the wild-type enzyme both in free form and in complex with acarbose
purified recombinant enzyme, microbatch technique by mixing of 0.0025 ml protein solution containing 10 mg/ml protein with 0.025 ml of precipitation solution, containing 80 mM sodium/potassium phosphate, pH 6.2, 8% PEG 3000, 4& PEG 3350, and 40 mM sodium thiocyanate, covering the mixture with 0.005 ml oil, 20°C, two weeks, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
His-tagged recombinant protein, to 2.85 A resolution, space group P3221, one protein molecule per asymmetric unit. One bound calcium ion is found, coordinated to the side chains of Asn100 and Asp167, the main-chains of Arg158 and His201, and three water molecules. The overall structure is the TIM barrel structure with two additional domains, domain B protruding out of the barrel in the place of the beta3-alpha3 loop and domain C succeeding the catalytic barrel
alpha-amylase complexed with alpha-cyclodextrin
enzyme complexed with 4-nitrophenyl alpha-D-maltoside, X-ray diffraction structure determination and analysis at 2.40 A resolution
sitting-drop vapour-diffusion method. The first crystal form is obtained by crystallization of BHA at room temperature in the presence of acarbose and maltose, resolution of 1.9 A. The crystal belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 47.0, b = 73.5, c = 151.1 A. The second crystal form is obtained by pH-induced crystallization of BHA in a MES-HEPES-boric acid buffer (MHB buffer) at 30°C. The solubility of BHA in MHB has a retrograde temperature dependency and crystallization of BHA is only possible by raising the temperature to at least 25°C. Data are collected at cryogenic temperature to a resolution of 2.0 A. The crystal belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 38.6, b = 59.0, c = 209.8 A
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purified recombinant TVAII mutant enzyme D325N complexed with alpha-panosylpanose, hanging drop vapour diffusion method, 0.0015 ml of 20 mg/ml protein in 5 m Tris-HCl, pH 7.5, is mixed with 0.0015 ml of reservoir solution containing 1% w/v PEG 6000, 5 mM CaCl2, and 40 mM MES-NaOH, pH 6.1, soaking of crystals in cryoprotection solution containing 20% v/v 2-methyl-2,4-pentanediol, 20% w/v PEG 6000, and 2.5 mM CaCl2, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling
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the circular dichroism spectrum shows two minima at 208 and 222 nm. Secondary structure analysis of the spectra estimated 31% alpha-helix, 15% beta-sheet, and 54% random coils
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