Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis.


Abstract

The thermal stability of the cold-active alpha-amylase (AHA) secreted by the Antarctic bacterium Alteromonas haloplanctis has been investigated by intrinsic fluorescence, circular dichroism, and differential scanning calorimetry. It was found that this heat-labile enzyme is the largest known multidomain protein exhibiting a reversible two-state unfolding, as demonstrated by the recovery of DeltaHcal values after consecutive calorimetric transitions, a DeltaHcal/DeltaHeff ratio close to unity, and the independence of unfolding thermodynamic parameters of scan rates. By contrast, the mesophilic alpha-amylases investigated here (from porcine pancreas, human salivary glands, yellow meal beetle, Bacillus amyloliquefaciens, and Bacillus licheniformis) unfold irreversibly according to a non-two-state mechanism. Unlike mesophilic alpha-amylases, the melting point of AHA is independent of calcium and chloride binding while the allosteric and structural functions of these ions are conserved. The thermostability of AHA at optimal conditions is characterized by a Tm of 43.7 degrees C, a DeltaHcal of 238 kcal mol-1, and a DeltaCp of 8.47 kcal mol-1 K-1. These values were used to calculate the Gibbs free energy of unfolding over a wide range of temperatures. This stability curve shows that (a) the specific DeltaGmax of AHA [22 cal (mol of residue)-1] is 4 times lower than that of mesophilic alpha-amylases, (b) group hydration plays a crucial role in the enzyme flexibility at low temperatures, (c) the temperature of cold unfolding closely corresponds to the lower limit of bacterial growth, and (d) the recombinant heat-labile enzyme can be expressed in mesophilic hosts at moderate temperatures. It is also argued that the cold-active alpha-amylase has evolved toward the lowest possible conformational stability of its native state. Study holds ProTherm entries: 5645, 5646, 5647, 5648, 5649, 5650, 5651, 5652, 5653, 5654, 5655, 5656, 5657, 5658, 5659, 5660, 5661, 5662, 5663, 5664, 5665, 5666, 5667 Extra Details:

Submission Details

ID: mYBtMV993

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:30 p.m.

Version: 1

Publication Details
Feller G;d'Amico D;Gerday C,Biochemistry (1999) Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. PMID:10194383
Additional Information

Study Summary

Number of data points 55
Proteins Pancreatic alpha-amylase ; GLYCOSYLTRANSFERASE ; Alpha-amylase ; Alpha-amylase ; Alpha-amylase 1 ; Alpha-amylase 1 ; Alpha-amylase ; Alpha-amylase ; Alpha-amylase
Unique complexes 6
Assays/Quantities/Protocols Experimental Assay: dHvH pH:7.2, buffers:MOPS: 30 mM ; Experimental Assay: dHcal buffers:MES: 30 mM, pH:6.4 ; Experimental Assay: Tm buffers:MES: 30 mM, pH:6.4 ; Experimental Assay: dHvH buffers:MES: 30 mM, pH:6.4 ; Experimental Assay: dHcal buffers:MES: 30 mM, pH:6.3 ; Experimental Assay: Tm buffers:MES: 30 mM, pH:6.3 ; Experimental Assay: dHvH buffers:MES: 30 mM, pH:6.3 ; Experimental Assay: dHcal pH:6.2, buffers:MES: 30 mM ; Experimental Assay: Tm pH:6.2, buffers:MES: 30 mM ; Experimental Assay: dHvH pH:6.2, buffers:MES: 30 mM ; Experimental Assay: dHcal buffers:MES: 30 mM, pH:6.1 ; Experimental Assay: Tm buffers:MES: 30 mM, pH:6.1 ; Experimental Assay: dHvH buffers:MES: 30 mM, pH:6.1 ; Experimental Assay: dHcal pH:6.0, buffers:MES: 30 mM ; Experimental Assay: Tm pH:6.0, buffers:MES: 30 mM ; Experimental Assay: dHvH pH:6.0, buffers:MES: 30 mM ; Experimental Assay: dHcal buffers:MES: 30 mM, pH:5.9 ; Experimental Assay: Tm buffers:MES: 30 mM, pH:5.9 ; Experimental Assay: dHvH buffers:MES: 30 mM, pH:5.9 ; Experimental Assay: dHcal pH:5.8, buffers:MES: 30 mM ; Experimental Assay: Tm pH:5.8, buffers:MES: 30 mM ; Experimental Assay: dHvH pH:5.8, buffers:MES: 30 mM ; Experimental Assay: dHcal pH:5.7, buffers:MES: 30 mM ; Experimental Assay: Tm pH:5.7, buffers:MES: 30 mM ; Experimental Assay: dHvH pH:5.7, buffers:MES: 30 mM ; Experimental Assay: dHcal pH:7.2, buffers:MOPS: 30 mM ; Experimental Assay: Tm pH:7.2, buffers:MOPS: 30 mM
Libraries Mutations for sequence QYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENVVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGSREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIKSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGSSILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVNGEDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWREIRNMVWFRNVVDGEPFANWWDNGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL ; Mutations for sequence TPTTFVHLFEWNWQDVAQECEQYLGPKGYAAVQVSPPNEHITGSQWWTRYQPVSYELQSRGGNRAQFIDMVNRCSAAGVDIYVDTLINHMAAGSGTGTAGNSFGNKSFPIYSPQDFHESCTINNSDYGNDRYRVQNCELVGLADLDTASNYVQNTIAAYINDLQAIGVKGFRFDASKHVAASDIQSLMAKVNGSPVVFQEVIDQGGEAVGASEYLSTGLVTEFKYSTELGNTFRNGSLAWLSNFGEGWGFMPSSSAVVFVDNHDNQRGHGGAGNVITFEDGRLYDLANVFMLAYPYGYPKVMSSYDFHGDTDAGGPNVPVHNNGNLECFASNWKCEHRWSYIAGGVDFRNNTADNWAVTNWWDNTNNQISFGRGSSGHMAINKEDSTLTATVQTDMASGQYCNVLKGELSADAKSCSGEVITVNSDGTINLNIGAWDAMAIHKNAKLNTSSAS ; Mutations for sequence MIQKRKRTVSFRLVLMCTLLFVSLPITKTSAVNGTLMQYFEWYTPNDGQHWKRLQNDAEHLSDIGITAVWIPPAYKGLSQSDNGYGPYDLYDLGEFQQKGTVRTKYGTKSELQDAIGSLHSRNVQVYGDVVLNHKAGADATEDVTAVEVNPANRNQETSEEYQIKAWTDFRFPGRGNTYSDFKWHWYHFDGADWDESRKISRIFKFRGEGKAWDWEVSSENGNYDYLMYADVDYDHPDVVAETKKWGIWYANELSLDGFRIDAAKHIKFSFLRDWVQAVRQATGKEMFTVAEYWQNNAGKLENYLNKTSFNQSVFDVPLHFNLQAASSQGGGYDMRRLLDGTVVSRHPEKAVTFVENHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQVFYGDMYGTKGTSPKEIPSLKDNIEPILKARKEYAYGPQHDYIDHPDVIGWTREGDSSAAKSGLAALITDGPGGSKRMYAGLKNAGETWYDITGNRSDTVKIGSDGWGEFHVNDGSVSIYVQK ; Mutations for sequence EYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL ; Mutations for sequence A:ANLNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQADVGYGAYDLYDLGEFHQKGTVRTKYGTKGELQSAIKSLHSRDINVYGDVVINHKGGADATEDVTAVEVDPADRNRVISGEHLIKAWTHFHFPGRGSTYSDFKWHWYHFDGTDWDESRKLNRIYKFQGKAWDWEVSNE/B:NGNYDYLMYADIDYDHPDVAAEIKRWGTWYANELQLDGFRLDAVKHIKFSFLRDWVNHVREKTGKEMFTVAEYWQNDLGALENYLNKTNFNHSVFDVPLHYQFHAASTQGGGYDMRKLLNSTVVSKHPLKAVTFVDNHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQVFYGDMYGTKGDSQREIPALKHKIEPILKARKQYAYGAQHDYFDHHDIVGWTREGDSSVANSGLAALITDGPGGAKRMYVGRQNAGETWHDITGNRSEPVVINSEGWGEFHVNGGSVSIYVQR ; Mutations for sequence EKDANFASGRNSIVHLFEWKWNDIADECERFLQPQGFGGVQISPPNEYLVADGRPWWERYQPVSYIINTRSGDESAFTDMTRRCNDAGVRIYVDAVINHMTGMNGVGTSGSSADHDGMNYPAVPYGSGDFHSPCEVNNYQDADNVRNCELVGLRDLNQGSDYVRGVLIDYMNHMIDLGVAGFRVDAAKHMSPGDLSVIFSGLKNLNTDYGFADGARPFIYQEVIDLGGEAISKNEYTGFGCVLEFQFGVSLGNAFQGGNQLKNLANWGPEWGLLEGLDAVVFVDNHDNQRTGGSQILTYKNPKPYKMAIAFMLAHPYGTTRIMSSFDFTDNDQGPPQDGSGNLISPGINDDNTCSNGYVCEHRWRQVYGMVGFRNAVEGTQVENWWSNDDNQIAFSRGSQGFVAFTNGGDLNQNLNTGLPAGTYCDVISGELSGGSCTGKSVTVGDNGSADISLGSAEDDGVLAIHVNAKL

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
5U3A 2017-12-06 0.95 Ultra High Resolution Crystal Structure of Human Pancreatic Alpha Amylase
4X9Y 2014-12-31 1.07 Wild-Type Human Pancreatic Alpha-Amylase at True Atomic Resolution (1.07 A)
4GQR 2012-10-24 1.2 Human Pancreatic alpha-amylase in complex with myricetin
5EMY 2016-07-06 1.23 Human Pancreatic Alpha-Amylase in complex with the mechanism based inactivator glucosyl epi-cyclophellitol
4W93 2015-07-15 1.35 Human pancreatic alpha-amylase in complex with montbretin A
4GQQ 2012-10-24 1.35 Human pancreatic alpha-amylase with bound ethyl caffeate
1HX0 2001-08-08 1.38 Structure of pig pancreatic alpha-amylase complexed with the 'truncate' acarbose molecule (pseudotrisaccharide)
3BH4 2008-12-09 1.4 High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase
5E0F 2016-09-07 1.4 Human pancreatic alpha-amylase in complex with mini-montbretin A
3IJ8 2009-10-27 1.43 Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase
3OLI 2011-04-13 1.5 Structures of human pancreatic alpha-amylase in complex with acarviostatin IV03
3DHP 2008-07-01 1.5 Probing the role of aromatic residues at the secondary saccharide binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding
3OLE 2011-04-13 1.55 Structures of human pancreatic alpha-amylase in complex with acarviostatin II03
3BLP 2008-11-18 1.6 Role of aromatic residues in human salivary alpha-amylase
1Z32 2005-05-31 1.6 Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues
1KXV 2002-06-19 1.6 Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase
1SMD 1996-07-11 1.6 HUMAN SALIVARY AMYLASE
1KXQ 2002-06-19 1.6 Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase
1JAE 1998-11-04 1.65 STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE
1VJS 1997-03-12 1.7 STRUCTURE OF ALPHA-AMYLASE PRECURSOR
1E43 2001-06-21 1.7 Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A
1G94 2001-12-12 1.74 CRYSTAL STRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE
1G9H 2002-06-26 1.8 TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL)
1HNY 1996-03-08 1.8 The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes
1OB0 2003-01-30 1.83 Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface
5KEZ 2017-03-29 1.83 Selective and potent inhibition of the glycosidase human amylase by the short and extremely compact peptide piHA from mRNA display
3IJ9 2009-10-27 1.85 Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase
1DHK 1997-12-24 1.85 STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE
1AQM 1999-03-02 1.85 ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS COMPLEXED WITH TRIS
1KBK 2002-04-10 1.9 Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
1KBB 2002-04-10 1.9 Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
1U30 2004-09-07 1.9 In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam
1XCX 2004-12-07 1.9 Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
3BAK 2008-03-25 1.9 N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate
3BAX 2008-03-25 1.9 N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide
1JXK 2001-09-14 1.9 Role of ethe mobile loop in the mehanism of human salivary amylase
3BAI 2008-03-25 1.9 Human Pancreatic Alpha Amylase with Bound Nitrate
1E3X 2001-06-21 1.9 Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.92A
1BLI 1999-03-23 1.9 BACILLUS LICHENIFORMIS ALPHA-AMYLASE
1E3Z 2001-06-21 1.93 Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A
1U2Y 2004-09-07 1.95 In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing D-gluconhydroximo-1,5-lactam
1U33 2004-09-07 1.95 In situ extension as an approach for identifying novel alpha-amylase inhibitors
3L2M 2010-04-14 1.97 X-ray Crystallographic Analysis of Pig Pancreatic Alpha-Amylase with Alpha-cyclodextrin
2QV4 2008-03-25 1.97 Human pancreatic alpha-amylase complexed with nitrite and acarbose
3BAY 2008-03-25 1.99 N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose
1JXJ 2001-09-14 1.99 Role of mobile loop in the mechanism of human salivary amylase
3IJ7 2009-10-27 2.0 Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase
1KXT 2002-06-19 2.0 Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase
3OLD 2011-04-13 2.0 Crystal structure of alpha-amylase in complex with acarviostatin I03
1XGZ 2005-05-24 2.0 Structure of the N298S variant of human pancreatic alpha-amylase
1XD0 2004-12-07 2.0 Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
1BSI 1999-05-18 2.0 HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN
2CPU 2001-06-30 2.0 SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
3CPU 2001-06-30 2.0 SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
1XCW 2004-12-07 2.0 Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
1MFV 2002-11-20 2.0 Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme
1XH0 2005-05-24 2.0 Structure of the N298S variant of human pancreatic alpha-amylase complexed with acarbose
1KGU 2002-01-16 2.0 THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337A VARIANT OF HUMAN PANCREATIC ALPHA-AMYLASE
3BAW 2008-03-25 2.0 Human pancreatic alpha-amylase complexed with azide
1AQH 1999-02-16 2.0 ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS
3BLK 2008-11-25 2.0 Role of aromatic residues in starch binding
1CLV 2000-05-03 2.0 YELLOW MEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR
1MFU 2002-11-20 2.0 Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant
1KGX 2002-01-16 2.0 Three Dimensional Structure Analysis of the R195Q Variant of Human Pancreatic Alpha Amylase
1CPU 1999-06-14 2.0 SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
1WO2 2005-03-15 2.01 Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion
1UA3 2003-10-14 2.01 Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides
1JFH 1998-12-02 2.03 STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION
1XH1 2005-05-24 2.03 Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride
1Q4N 2004-03-16 2.07 Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity
1NM9 2004-01-20 2.1 Crystal structure of recombinant human salivary amylase mutant W58A
3BAJ 2008-03-25 2.1 Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose
1KGW 2002-01-16 2.1 THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT OF HUMAN PANCREATIC ALPHA-MYLASE
1L0P 2002-06-19 2.1 CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS AND NITRATE
1KB3 2002-05-01 2.1 Three Dimensional Structure Analysis of the R195A Variant of Human Pancreatic Alpha Amylase
3L2L 2010-04-14 2.11 X-ray Crystallographic Analysis of Pig Pancreatic Alpha-Amylase with Limit Dextrin and Oligosaccharide
1BPL 1996-08-17 2.2 GLYCOSYLTRANSFERASE
1PPI 1995-05-24 2.2 THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS RESOLUTION
1XD1 2004-12-07 2.2 Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
1PIG 1996-12-07 2.2 PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE OLIGOSACCHARIDE V-1532
1E40 2001-06-21 2.2 Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A
1XH2 2005-05-24 2.2 Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose
1JD7 2002-09-18 2.25 CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT K300R OF PSEUDOALTEROMONAS HALOPLANCTIS ALPHA-AMYLASE
1KXH 2002-06-19 2.3 Crystal structure of the complex between an inactive mutant of psychrophilic alpha-amylase (D174N) and acarbose
1PIF 1996-12-07 2.3 PIG ALPHA-AMYLASE
1OSE 1997-04-01 2.3 Porcine pancreatic alpha-amylase complexed with acarbose
3OLG 2011-04-13 2.3 Structures of human pancreatic alpha-amylase in complex with acarviostatin III03
2QMK 2008-03-25 2.3 Human pancreatic alpha-amylase complexed with nitrite
5TD4 2016-11-02 2.3 Starch binding sites on the Human pancreatic alpha amylase D300N variant complexed with an octaose substrate.
1C8Q 2001-06-13 2.3 STRUCTURE SOLUTION AND REFINEMENT OF THE RECOMBINANT HUMAN SALIVARY AMYLASE
1VAH 2005-04-26 2.4 Crystal structure of the pig pancreatic-amylase complexed with r-nitrophenyl-a-D-maltoside
1B0I 1999-11-17 2.4 ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS
1TMQ 1999-03-02 2.5 STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR
1BVN 1998-09-23 2.5 PIG PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE PROTEINACEOUS INHIBITOR TENDAMISTAT
1JD9 2002-09-18 2.5 CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT K300Q OF PSEUDOALTEROMONAS HALOPLANCTIS ALPHA-AMYLASE
5VA9 2018-03-28 2.55 Human pancreatic alpha amylase in complex with peptide inhibitor piHA-L5(d10Y)
4X0N 2015-11-25 2.6 Porcine pancreatic alpha-amylase in complex with helianthamide, a novel proteinaceous inhibitor
1XV8 2005-10-11 3.0 Crystal Structure of Human Salivary Alpha-Amylase Dimer
1VIW 1999-07-22 3.0 TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX
1B2Y 2000-02-16 3.2 STRUCTURE OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
98.4 Pancreatic alpha-amylase P00690 AMYP_PIG
197.4 A,B GLYCOSYLTRANSFERASE P06278 AMY_BACLI
100.0 Alpha-amylase P56634 AMY_TENMO
100.0 Alpha-amylase P00692 AMY_BACAM
97.0 Alpha-amylase 1 P04746 AMYP_HUMAN
97.6 Alpha-amylase 1 P19961 AMY2B_HUMAN
100.0 Alpha-amylase 1 P04745 AMY1_HUMAN
100.0 Alpha-amylase P29957 AMY_PSEHA