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Pancreatic alpha-amylase (PA) (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase)

 AMYP_PIG                Reviewed;         511 AA.
P00690; Q9TUE4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
15-AUG-2003, sequence version 3.
12-SEP-2018, entry version 162.
RecName: Full=Pancreatic alpha-amylase;
Short=PA;
EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
Flags: Precursor;
Name=AMY2;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
PubMed=10082956; DOI=10.1016/S0167-4838(99)00011-4;
Darnis S., Juge N., Guo X.-J., Marchis-Mouren G., Puigserver A.,
Chaix J.-C.;
"Molecular cloning and primary structure analysis of porcine
pancreatic alpha-amylase.";
Biochim. Biophys. Acta 1430:281-289(1999).
[2]
PROTEIN SEQUENCE OF 16-511, AND DISULFIDE BONDS.
PubMed=3484639; DOI=10.1016/0167-4838(86)90289-X;
Pasero L., Mazzei-Pierron Y., Abadie B., Chicheportiche Y.,
Marchis-Mouren G.;
"Complete amino acid sequence and location of the five disulfide
bridges in porcine pancreatic alpha-amylase.";
Biochim. Biophys. Acta 869:147-157(1986).
[3]
DISULFIDE BONDS.
PubMed=6188459; DOI=10.1016/0006-291X(83)91021-5;
Pasero L., Mazzei Y., Abadie B., Moinier D., Fougereau M.,
Marchis-Mouren G.;
"Localization of the two free thiol groups in the porcine pancreatic
alpha-amylase I sequence.";
Biochem. Biophys. Res. Commun. 110:726-732(1983).
[4]
X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS).
Payan F., Haser R., Pierrot M., Frey M., Astier J.-P., Abadie B.,
Duee E., Buisson G.;
"The three-dimensional structure of alpha-amylase from porcine
pancreas at 5-A resolution -- the active-site location.";
Acta Crystallogr. B 36:416-421(1980).
[5]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, AND DISULFIDE BONDS.
PubMed=3502087;
Buisson G., Duee E., Haser R., Payan F.;
"Three dimensional structure of porcine pancreatic alpha-amylase at
2.9-A resolution. Role of calcium in structure and activity.";
EMBO J. 6:3909-3916(1987).
[6]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION.
PubMed=8515451; DOI=10.1006/jmbi.1993.1326;
Qian M., Haser R., Payan F.;
"Structure and molecular model refinement of pig pancreatic alpha-
amylase at 2.1-A resolution.";
J. Mol. Biol. 231:785-799(1993).
[7]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 16-511 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, AND COFACTOR.
PubMed=8193143; DOI=10.1021/bi00186a031;
Qian M., Haser R., Buisson G., Duee E., Payan F.;
"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.";
Biochemistry 33:6284-6294(1994).
[8]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH
INHIBITOR; CALCIUM AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR.
PubMed=7897663; DOI=10.1006/jmbi.1994.0125;
Wiegand G., Epp O., Huber R.;
"The crystal structure of porcine pancreatic alpha-amylase in complex
with the microbial inhibitor Tendamistat.";
J. Mol. Biol. 247:99-110(1995).
[9]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH
CALCIUM; GLUCOSE AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR.
PubMed=8757803; DOI=10.1006/jmbi.1996.0410;
Machius M., Vertesy L., Huber R., Wiegand G.;
"Carbohydrate and protein-based inhibitors of porcine pancreatic
alpha-amylase: structure analysis and comparison of their binding
characteristics.";
J. Mol. Biol. 260:409-421(1996).
[10]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 17-511 IN COMPLEX WITH
CALCIUM, SEQUENCE REVISION, COFACTOR, AND DISULFIDE BONDS.
PubMed=8681972; DOI=10.1111/j.1432-1033.1996.0561z.x;
Gilles C., Astier J.-P., Marchis-Mouren G., Cambillau C., Payan F.;
"Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in
complex with the carbohydrate inhibitor acarbose.";
Eur. J. Biochem. 238:561-569(1996).
[11]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 17-511 IN COMPLEX WITH
INHIBITOR AND CALCIUM, COFACTOR, AND DISULFIDE BONDS.
PubMed=8994970; DOI=10.1016/S0969-2126(96)00151-7;
Bompard-Gilles C., Rousseau P., Rouge P., Payan F.;
"Substrate mimicry in the active center of a mammalian alpha-amylase:
structural analysis of an enzyme-inhibitor complex.";
Structure 4:1441-1452(1996).
[12]
X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH
CALCIUM AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR.
PubMed=9385631; DOI=10.1002/pro.5560061102;
Qian M., Spinelli S., Driguez H., Payan F.;
"Structure of a pancreatic alpha-amylase bound to a substrate analogue
at 2.03-A resolution.";
Protein Sci. 6:2285-2296(1997).
[13]
X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM;
CHLORIDE AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, AND DISULFIDE BOND.
PubMed=11412124; DOI=10.1021/bi0102050;
Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.;
"Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase.
High-resolution structural analysis of an enzyme-inhibitor complex.";
Biochemistry 40:7700-7709(2001).
[14]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH
CALCIUM AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR.
PubMed=11960990; DOI=10.1074/jbc.M202327200;
Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L.,
Muyldermans S., Cambillau C.;
"Three camelid VHH domains in complex with porcine pancreatic alpha-
amylase. Inhibition and versatility of binding topology.";
J. Biol. Chem. 277:23645-23650(2002).
-!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
linkages in polysaccharides containing three or more (1->4)-alpha-
linked D-glucose units. {ECO:0000250|UniProtKB:P04746}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087,
ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087,
ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631};
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996;
Evidence={ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087,
ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:9385631};
Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087,
ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:9385631};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- MISCELLANEOUS: The two forms of this enzyme, I and II, show very
similar activities, molecular masses, and compositions and differ
only in their isoelectric points. As no evidence for two variants
were in the cDNA library of PubMed:10082956, it is most likely
that isoform I (PPAI) and isoform II (PPAII) are two forms of the
same protein.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/AA/";
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EMBL; AF064742; AAF02828.1; -; mRNA.
PIR; A25412; ALPGP.
RefSeq; NP_999360.1; NM_214195.1.
UniGene; Ssc.94418; -.
PDB; 1BVN; X-ray; 2.50 A; P=16-511.
PDB; 1DHK; X-ray; 1.85 A; A=17-511.
PDB; 1HX0; X-ray; 1.38 A; A=16-511.
PDB; 1JFH; X-ray; 2.03 A; A=17-511.
PDB; 1KXQ; X-ray; 1.60 A; A/B/C/D=16-511.
PDB; 1KXT; X-ray; 2.00 A; A/C/E=16-511.
PDB; 1KXV; X-ray; 1.60 A; A/B=16-511.
PDB; 1OSE; X-ray; 2.30 A; A=17-511.
PDB; 1PIF; X-ray; 2.30 A; A=17-511.
PDB; 1PIG; X-ray; 2.20 A; A=17-511.
PDB; 1PPI; X-ray; 2.20 A; A=16-511.
PDB; 1UA3; X-ray; 2.01 A; A=16-511.
PDB; 1VAH; X-ray; 2.40 A; A=16-511.
PDB; 1WO2; X-ray; 2.01 A; A=16-511.
PDB; 3L2L; X-ray; 2.11 A; A=16-511.
PDB; 3L2M; X-ray; 1.97 A; A=16-511.
PDB; 4X0N; X-ray; 2.60 A; A=17-511.
PDBsum; 1BVN; -.
PDBsum; 1DHK; -.
PDBsum; 1HX0; -.
PDBsum; 1JFH; -.
PDBsum; 1KXQ; -.
PDBsum; 1KXT; -.
PDBsum; 1KXV; -.
PDBsum; 1OSE; -.
PDBsum; 1PIF; -.
PDBsum; 1PIG; -.
PDBsum; 1PPI; -.
PDBsum; 1UA3; -.
PDBsum; 1VAH; -.
PDBsum; 1WO2; -.
PDBsum; 3L2L; -.
PDBsum; 3L2M; -.
PDBsum; 4X0N; -.
ProteinModelPortal; P00690; -.
SMR; P00690; -.
MINT; P00690; -.
STRING; 9823.ENSSSCP00000026998; -.
BindingDB; P00690; -.
ChEMBL; CHEMBL5730; -.
Allergome; 970; Sus s Amylase.
CAZy; GH13; Glycoside Hydrolase Family 13.
PaxDb; P00690; -.
PeptideAtlas; P00690; -.
PRIDE; P00690; -.
GeneID; 397397; -.
KEGG; ssc:397397; -.
CTD; 397397; -.
eggNOG; KOG2212; Eukaryota.
eggNOG; COG0366; LUCA.
HOGENOM; HOG000253313; -.
HOVERGEN; HBG000061; -.
InParanoid; P00690; -.
KO; K01176; -.
BRENDA; 3.2.1.1; 6170.
SABIO-RK; P00690; -.
EvolutionaryTrace; P00690; -.
PRO; PR:P00690; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0004556; F:alpha-amylase activity; ISS:UniProtKB.
GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB.
Gene3D; 2.60.40.1180; -; 1.
InterPro; IPR006048; A-amylase/branching_C.
InterPro; IPR031319; A-amylase_C.
InterPro; IPR006046; Alpha_amylase.
InterPro; IPR006047; Glyco_hydro_13_cat_dom.
InterPro; IPR013780; Glyco_hydro_b.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00128; Alpha-amylase; 1.
Pfam; PF02806; Alpha-amylase_C; 1.
PRINTS; PR00110; ALPHAAMYLASE.
SMART; SM00642; Aamy; 1.
SMART; SM00632; Aamy_C; 1.
SUPFAM; SSF51445; SSF51445; 1.
1: Evidence at protein level;
3D-structure; Calcium; Carbohydrate metabolism; Chloride;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
SIGNAL 1 15 {ECO:0000269|PubMed:3484639}.
CHAIN 16 511 Pancreatic alpha-amylase.
/FTId=PRO_0000001399.
ACT_SITE 212 212 Nucleophile.
ACT_SITE 248 248 Proton donor.
METAL 115 115 Calcium. {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970,
ECO:0000269|PubMed:9385631}.
METAL 173 173 Calcium; via carbonyl oxygen.
{ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970,
ECO:0000269|PubMed:9385631}.
METAL 182 182 Calcium. {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970,
ECO:0000269|PubMed:9385631}.
METAL 216 216 Calcium; via carbonyl oxygen.
{ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970,
ECO:0000269|PubMed:9385631}.
BINDING 210 210 Chloride. {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:9385631}.
BINDING 313 313 Chloride. {ECO:0000305}.
BINDING 352 352 Chloride. {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:9385631}.
SITE 315 315 Transition state stabilizer.
{ECO:0000250|UniProtKB:P04746}.
MOD_RES 16 16 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P04746}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine.
DISULFID 43 101 {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970,
ECO:0000269|PubMed:9385631,
ECO:0000305|PubMed:3502087}.
DISULFID 85 130 {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970,
ECO:0000269|PubMed:9385631,
ECO:0000305|PubMed:3502087}.
DISULFID 156 175 {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970,
ECO:0000269|PubMed:9385631,
ECO:0000305|PubMed:3502087}.
DISULFID 393 399 {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970,
ECO:0000269|PubMed:9385631,
ECO:0000305|PubMed:3502087}.
DISULFID 465 477 {ECO:0000269|PubMed:11412124,
ECO:0000269|PubMed:11960990,
ECO:0000269|PubMed:7897663,
ECO:0000269|PubMed:8193143,
ECO:0000269|PubMed:8681972,
ECO:0000269|PubMed:8757803,
ECO:0000269|PubMed:8994970,
ECO:0000269|PubMed:9385631,
ECO:0000305|PubMed:3502087}.
CONFLICT 138 138 N -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 367 367 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 405 405 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 419 419 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 426 426 A -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 27 31 {ECO:0000244|PDB:1HX0}.
HELIX 36 45 {ECO:0000244|PDB:1HX0}.
TURN 46 51 {ECO:0000244|PDB:1HX0}.
STRAND 54 57 {ECO:0000244|PDB:1HX0}.
TURN 67 70 {ECO:0000244|PDB:1HX0}.
HELIX 73 77 {ECO:0000244|PDB:1HX0}.
STRAND 78 80 {ECO:0000244|PDB:1HX0}.
STRAND 84 86 {ECO:0000244|PDB:1PIF}.
HELIX 91 103 {ECO:0000244|PDB:1HX0}.
STRAND 107 112 {ECO:0000244|PDB:1HX0}.
STRAND 115 119 {ECO:0000244|PDB:1HX0}.
STRAND 124 126 {ECO:0000244|PDB:1KXQ}.
STRAND 128 130 {ECO:0000244|PDB:1HX0}.
HELIX 136 138 {ECO:0000244|PDB:1HX0}.
TURN 142 145 {ECO:0000244|PDB:1HX0}.
HELIX 148 150 {ECO:0000244|PDB:1HX0}.
TURN 153 155 {ECO:0000244|PDB:1HX0}.
STRAND 158 162 {ECO:0000244|PDB:1KXV}.
HELIX 169 174 {ECO:0000244|PDB:1HX0}.
STRAND 175 177 {ECO:0000244|PDB:1HX0}.
STRAND 180 183 {ECO:0000244|PDB:1HX0}.
HELIX 188 204 {ECO:0000244|PDB:1HX0}.
STRAND 208 211 {ECO:0000244|PDB:1HX0}.
HELIX 214 216 {ECO:0000244|PDB:1HX0}.
HELIX 219 226 {ECO:0000244|PDB:1HX0}.
TURN 234 236 {ECO:0000244|PDB:1HX0}.
STRAND 244 247 {ECO:0000244|PDB:1HX0}.
STRAND 253 257 {ECO:0000244|PDB:1HX0}.
HELIX 259 262 {ECO:0000244|PDB:1HX0}.
TURN 263 265 {ECO:0000244|PDB:1HX0}.
STRAND 266 269 {ECO:0000244|PDB:1HX0}.
HELIX 272 281 {ECO:0000244|PDB:1HX0}.
HELIX 289 294 {ECO:0000244|PDB:1HX0}.
HELIX 297 299 {ECO:0000244|PDB:1HX0}.
HELIX 304 306 {ECO:0000244|PDB:1HX0}.
STRAND 307 309 {ECO:0000244|PDB:1HX0}.
HELIX 316 318 {ECO:0000244|PDB:1HX0}.
STRAND 319 321 {ECO:0000244|PDB:1KXQ}.
HELIX 324 326 {ECO:0000244|PDB:1HX0}.
HELIX 330 332 {ECO:0000244|PDB:1HX0}.
HELIX 333 345 {ECO:0000244|PDB:1HX0}.
STRAND 348 355 {ECO:0000244|PDB:1HX0}.
STRAND 363 366 {ECO:0000244|PDB:3L2M}.
TURN 369 372 {ECO:0000244|PDB:1HX0}.
STRAND 375 378 {ECO:0000244|PDB:1HX0}.
HELIX 400 402 {ECO:0000244|PDB:1HX0}.
HELIX 404 415 {ECO:0000244|PDB:1HX0}.
TURN 416 418 {ECO:0000244|PDB:1HX0}.
STRAND 421 426 {ECO:0000244|PDB:1HX0}.
STRAND 428 436 {ECO:0000244|PDB:1HX0}.
TURN 437 439 {ECO:0000244|PDB:1HX0}.
STRAND 440 445 {ECO:0000244|PDB:1HX0}.
STRAND 447 449 {ECO:0000244|PDB:1HX0}.
STRAND 451 456 {ECO:0000244|PDB:1HX0}.
STRAND 461 465 {ECO:0000244|PDB:1HX0}.
TURN 467 469 {ECO:0000244|PDB:1HX0}.
STRAND 476 479 {ECO:0000244|PDB:1HX0}.
STRAND 481 484 {ECO:0000244|PDB:1HX0}.
STRAND 488 494 {ECO:0000244|PDB:1HX0}.
STRAND 498 500 {ECO:0000244|PDB:1KXQ}.
STRAND 502 506 {ECO:0000244|PDB:1HX0}.
HELIX 507 509 {ECO:0000244|PDB:1HX0}.
SEQUENCE 511 AA; 57086 MW; 117489E020807378 CRC64;
MKLFLLLSAF GFCWAQYAPQ TQSGRTSIVH LFEWRWVDIA LECERYLGPK GFGGVQVSPP
NENIVVTNPS RPWWERYQPV SYKLCTRSGN ENEFRDMVTR CNNVGVRIYV DAVINHMCGS
GAAAGTGTTC GSYCNPGNRE FPAVPYSAWD FNDGKCKTAS GGIESYNDPY QVRDCQLVGL
LDLALEKDYV RSMIADYLNK LIDIGVAGFR IDASKHMWPG DIKAVLDKLH NLNTNWFPAG
SRPFIFQEVI DLGGEAIQSS EYFGNGRVTE FKYGAKLGTV VRKWSGEKMS YLKNWGEGWG
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKVAV GFMLAHPYGF TRVMSSYRWA
RNFVNGQDVN DWIGPPNNNG VIKEVTINAD TTCGNDWVCE HRWRQIRNMV WFRNVVDGQP
FANWWANGSN QVAFGRGNRG FIVFNNDDWQ LSSTLQTGLP GGTYCDVISG DKVGNSCTGI
KVYVSSDGTA QFSISNSAED PFIAIHAESK L


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E1454p ELISA kit 1,4-alpha-D-glucan glucanohydrolase,AMY2,PA,Pancreatic alpha-amylase,Pig,Sus scrofa 96T
E1454p ELISA 1,4-alpha-D-glucan glucanohydrolase,AMY2,PA,Pancreatic alpha-amylase,Pig,Sus scrofa 96T
E1454r ELISA 1,4-alpha-D-glucan glucanohydrolase,Amy2,PA,Pancreatic alpha-amylase,Rat,Rattus norvegicus 96T
E1454r ELISA kit 1,4-alpha-D-glucan glucanohydrolase,Amy2,PA,Pancreatic alpha-amylase,Rat,Rattus norvegicus 96T
U1454r CLIA 1,4-alpha-D-glucan glucanohydrolase,Amy2,PA,Pancreatic alpha-amylase,Rat,Rattus norvegicus 96T
E1454m ELISA kit 1,4-alpha-D-glucan glucanohydrolase,Amy2,Amy2a,Mouse,Mus musculus,PA,Pancreatic alpha-amylase 96T
U1454h CLIA 1,4-alpha-D-glucan glucanohydrolase,AMY2A,Homo sapiens,Human,PA,Pancreatic alpha-amylase 96T
E1454m ELISA 1,4-alpha-D-glucan glucanohydrolase,Amy2,Amy2a,Mouse,Mus musculus,PA,Pancreatic alpha-amylase 96T
U1454m CLIA 1,4-alpha-D-glucan glucanohydrolase,Amy2,Amy2a,Mouse,Mus musculus,PA,Pancreatic alpha-amylase 96T
E1454h ELISA 1,4-alpha-D-glucan glucanohydrolase,AMY2A,Homo sapiens,Human,PA,Pancreatic alpha-amylase 96T
E1454h ELISA kit 1,4-alpha-D-glucan glucanohydrolase,AMY2A,Homo sapiens,Human,PA,Pancreatic alpha-amylase 96T
U1482h CLIA 1,4-alpha-D-glucan glucanohydrolase 1,Alpha-amylase 1,AMY1,AMY1A,Homo sapiens,Human,Salivary alpha-amylase 96T
U1482m CLIA 1,4-alpha-D-glucan glucanohydrolase 1,Alpha-amylase 1,Amy1,Amy1a,Amy-1-a,Mouse,Mus musculus,Salivary and hepatic alpha-amylase 96T
E1482h ELISA 1,4-alpha-D-glucan glucanohydrolase 1,Alpha-amylase 1,AMY1,AMY1A,Homo sapiens,Human,Salivary alpha-amylase 96T
E1482m ELISA 1,4-alpha-D-glucan glucanohydrolase 1,Alpha-amylase 1,Amy1,Amy1a,Amy-1-a,Mouse,Mus musculus,Salivary and hepatic alpha-amylase 96T
E1482h ELISA kit 1,4-alpha-D-glucan glucanohydrolase 1,Alpha-amylase 1,AMY1,AMY1A,Homo sapiens,Human,Salivary alpha-amylase 96T
E1482m ELISA kit 1,4-alpha-D-glucan glucanohydrolase 1,Alpha-amylase 1,Amy1,Amy1a,Amy-1-a,Mouse,Mus musculus,Salivary and hepatic alpha-amylase 96T
CI36 Recombinant Human Alpha-amylase 2B_1,4-alpha-D-glucan glucanohydrolase 2B_Carcinoid alpha-amylase 1 mg
CI36 Recombinant Human Alpha-amylase 2B_1,4-alpha-D-glucan glucanohydrolase 2B_Carcinoid alpha-amylase 500 ug
CI36 Recombinant Human Alpha-amylase 2B_1,4-alpha-D-glucan glucanohydrolase 2B_Carcinoid alpha-amylase 50 ug
CI36 Recombinant Human Alpha-amylase 2B_1,4-alpha-D-glucan glucanohydrolase 2B_Carcinoid alpha-amylase 10 ug
18-783-77298 SHEEP ANTI HUMAN AMYLASE (SALIVARY) - EC 3.2.1.1; PA; 1.4-alpha-D-glucan glucanohydrolase Polyclonal 1 ml
120-15 ALPHA-AMYLASE (a-Amylase), Human Pancreatic - Liquid - High Purity Liquid 100 units
120-15 ALPHA-AMYLASE (a-Amylase), Human Pancreatic - Liquid - High Purity Liquid 25 units


 

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