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Alpha-galactosidase (EC 3.2.1.22) (Melibiase)

 AGAL_THEMA              Reviewed;         552 AA.
G4FEF4; O33835;
15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
07-NOV-2018, entry version 58.
RecName: Full=Alpha-galactosidase {ECO:0000303|PubMed:9741105, ECO:0000312|EMBL:AGL50123.1, ECO:0000312|EMBL:CAA04514.1};
EC=3.2.1.22 {ECO:0000269|PubMed:17323919, ECO:0000269|PubMed:24237145, ECO:0000269|PubMed:25486100, ECO:0000269|PubMed:26005928, ECO:0000269|PubMed:27783466, ECO:0000269|PubMed:9741105};
AltName: Full=Melibiase {ECO:0000305};
Name=galA {ECO:0000303|PubMed:9741105, ECO:0000312|EMBL:CAA04514.1};
OrderedLocusNames=TM_1192 {ECO:0000312|EMBL:AAD36267.1};
ORFNames=Tmari_1199 {ECO:0000312|EMBL:AGL50123.1};
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
NCBI_TaxID=243274 {ECO:0000312|EMBL:AGL50123.1};
[1] {ECO:0000312|EMBL:CAA04514.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-36, FUNCTION,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
SPECIFICITY, SUBUNIT, AND OPERON STRUCTURE.
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
{ECO:0000312|EMBL:CAA04514.1};
PubMed=9741105;
Liebl W., Wagner B., Schellhase J.;
"Properties of an alpha-galactosidase, and structure of its gene galA,
within an alpha- and beta-galactoside utilization gene cluster of the
hyperthermophilic bacterium Thermotoga maritima.";
Syst. Appl. Microbiol. 21:1-11(1998).
[2] {ECO:0000312|EMBL:AAD36267.1, ECO:0000312|Proteomes:UP000008183}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
{ECO:0000312|EMBL:AAD36267.1, ECO:0000312|Proteomes:UP000008183};
PubMed=10360571; DOI=10.1038/20601;
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
"Evidence for lateral gene transfer between Archaea and Bacteria from
genome sequence of Thermotoga maritima.";
Nature 399:323-329(1999).
[3] {ECO:0000312|EMBL:AGL50123.1, ECO:0000312|Proteomes:UP000013901}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
{ECO:0000312|EMBL:AGL50123.1, ECO:0000312|Proteomes:UP000013901};
PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
Zengler K.;
"The genome organization of Thermotoga maritima reflects its
lifestyle.";
PLoS Genet. 9:E1003485-E1003485(2013).
[4]
CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS
OF ASP-220; ASP-327 AND ASP-387.
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
{ECO:0000303|PubMed:17323919};
PubMed=17323919; DOI=10.1021/bi061521n;
Comfort D.A., Bobrov K.S., Ivanen D.R., Shabalin K.A., Harris J.M.,
Kulminskaya A.A., Brumer H., Kelly R.M.;
"Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase
(TmGalA) confirms the mechanistic commonality of clan GH-D glycoside
hydrolases.";
Biochemistry 46:3319-3330(2007).
[5]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
PHE-328; GLY-385 AND PRO-402, AND PROTEIN ENGINEERING.
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
{ECO:0000303|PubMed:24237145};
PubMed=24237145; DOI=10.1134/S0006297913100052;
Bobrov K.S., Borisova A.S., Eneyskaya E.V., Ivanen D.R.,
Shabalin K.A., Kulminskaya A.A., Rychkov G.N.;
"Improvement of the efficiency of transglycosylation catalyzed by
alpha-galactosidase from Thermotoga maritima by protein engineering.";
Biochemistry (Mosc.) 78:1112-1123(2013).
[6]
CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
{ECO:0000303|PubMed:26005928};
PubMed=26005928; DOI=10.1016/j.carres.2015.03.021;
Borisova A.S., Reddy S.K., Ivanen D.R., Bobrov K.S., Eneyskaya E.V.,
Rychkov G.N., Sandgren M., Staalbrand H., Sinnott M.L.,
Kulminskaya A.A., Shabalin K.A.;
"The method of integrated kinetics and its applicability to the exo-
glycosidase-catalyzed hydrolysis of p-nitrophenyl glycosides.";
Carbohydr. Res. 412:43-49(2015).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
{ECO:0000303|PubMed:25486100};
PubMed=25486100; DOI=10.1016/j.carres.2014.11.003;
Borisova A.S., Ivanen D.R., Bobrov K.S., Eneyskaya E.V., Rychkov G.N.,
Sandgren M., Kulminskaya A.A., Sinnott M.L., Shabalin K.A.;
"alpha-Galactobiosyl units: thermodynamics and kinetics of their
formation by transglycosylations catalysed by the GH36 alpha-
galactosidase from Thermotoga maritima.";
Carbohydr. Res. 401:115-121(2015).
[8] {ECO:0000244|PDB:1ZY9}
X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF APOENZYME.
Joint Center for Structural Genomics (JCSG);
"Crystal structure of alpha-galactosidase (ec 3.2.1.22) (melibiase)
(tm1192) from Thermotoga maritima at 2.34 A resolution.";
Submitted (JUN-2005) to the PDB data bank.
[9] {ECO:0000244|PDB:5M0X, ECO:0000244|PDB:5M12, ECO:0000244|PDB:5M16, ECO:0000244|PDB:5M1I}
X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF SUBSTRATE-FREE ENZYME AND IN
COMPLEX WITH INHIBITOR ANALOG AND HYDROLYSIS PRODUCT, CATALYTIC
ACTIVITY, ACTIVITY REGULATION, AND REACTION MECHANISM.
PubMed=27783466; DOI=10.1002/anie.201607431;
Adamson C., Pengelly R.J., Shamsi Kazem Abadi S., Chakladar S.,
Draper J., Britton R., Gloster T.M., Bennet A.J.;
"Structural snapshots for mechanism-based inactivation of a glycoside
hydrolase by cyclopropyl carbasugars.";
Angew. Chem. Int. Ed. 55:14978-14982(2016).
-!- FUNCTION: Hydrolyzes the short-chain alpha-galactosaccharides
raffinose, melibiose and stachyose. {ECO:0000269|PubMed:25486100,
ECO:0000269|PubMed:9741105}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing alpha-D-
galactose residues in alpha-D-galactosides, including galactose
oligosaccharides, galactomannans and galactolipids.
{ECO:0000269|PubMed:17323919, ECO:0000269|PubMed:24237145,
ECO:0000269|PubMed:25486100, ECO:0000269|PubMed:26005928,
ECO:0000269|PubMed:27783466, ECO:0000269|PubMed:9741105}.
-!- ACTIVITY REGULATION: Inhibited by hydrolyzation product alpha-
galactopyranose and to a lesser extent by beta-galactopyranose,
its mutarotational product (PubMed:26005928). Inhibited by
synthetic cyclopropyl carbasugars (PubMed:27783466).
{ECO:0000269|PubMed:26005928, ECO:0000269|PubMed:27783466}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.075 mM for p-nitrophenol-alpha-galactoside (at pH 5.0 and
75 degrees Celsius) {ECO:0000269|PubMed:9741105};
KM=2.100 mM for raffinose (at pH 5.0 and 75 degrees Celsius)
{ECO:0000269|PubMed:9741105};
KM=0.110 mM for p-nitrophenyl-alpha-D-galactopyranoside (at pH
5.0 and 37 degrees Celsius) {ECO:0000269|PubMed:24237145};
KM=1.170 mM for melibiose (at pH 5.0 and 37 degrees Celsius)
{ECO:0000269|PubMed:25486100};
KM=10.040 mM for raffinose (at pH 5.0 and 37 degrees Celsius)
{ECO:0000269|PubMed:25486100};
KM=2.840 mM for stachyose (at pH 5.0 and 37 degrees Celsius)
{ECO:0000269|PubMed:25486100};
Vmax=166 umol/min/mg enzyme for 4-nitrophenol-alpha-galactoside
(at pH 5.0 and 75 degrees Celsius) {ECO:0000269|PubMed:9741105};
Vmax=103 umol/min/mg enzyme for raffinose (at pH 5.0 and 75
degrees Celsius) {ECO:0000269|PubMed:9741105};
Note=kcat is 176 s(1) for p-nitrophenol-alpha-galactoside (at pH
5.0 and 75 degrees Celsius). kcat is 109 s(1) for raffinose (at
pH 5.0 and 75 degrees Celsius) (PubMed:9741105). kcat is 8 s(1)
for p-nitrophenyl-alpha-D-galactopyranoside (at pH 5.0 and 37
degrees Celsius) (PubMed:24237145). kcat is 2.33 s(1) for
melibiose (at pH 5.0 and 37 degrees Celsius). kcat is 5.0 s(1)
for raffinose (at pH 5.0 and 37 degrees Celsius). kcat is 0.53
s(1) for stachyose (at pH 5.0 and 37 degrees Celsius)
(PubMed:25486100). {ECO:0000269|PubMed:24237145,
ECO:0000269|PubMed:25486100, ECO:0000269|PubMed:9741105};
pH dependence:
Optimum pH is 5.0-5.5 when using synthetic substrate p-
nitrophenyl-alpha-D-galactopyranoside.
{ECO:0000269|PubMed:9741105};
Temperature dependence:
Optimum temperature is 90-95 degrees Celsius when using
synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside. The
half-life of thermoinactivation is 6.5 h at 85 degrees Celsius.
{ECO:0000269|PubMed:9741105};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9741105}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family.
{ECO:0000305}.
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EMBL; AJ001072; CAA04514.1; -; Genomic_DNA.
EMBL; AE000512; AAD36267.1; -; Genomic_DNA.
EMBL; CP004077; AGL50123.1; -; Genomic_DNA.
PIR; E72283; E72283.
RefSeq; NP_228997.1; NC_000853.1.
RefSeq; WP_004080136.1; NZ_CP011107.1.
PDB; 1ZY9; X-ray; 2.34 A; A=1-552.
PDB; 5M0X; X-ray; 1.80 A; A=1-552.
PDB; 5M12; X-ray; 1.53 A; A=1-552.
PDB; 5M16; X-ray; 1.62 A; A=1-552.
PDB; 5M1I; X-ray; 1.55 A; A=1-552.
PDB; 6GTA; X-ray; 2.20 A; A=1-552.
PDB; 6GVD; X-ray; 1.22 A; A=1-552.
PDB; 6GWF; X-ray; 1.72 A; A=1-552.
PDB; 6GWG; X-ray; 1.77 A; A=1-552.
PDB; 6GX8; X-ray; 1.42 A; A=1-552.
PDBsum; 1ZY9; -.
PDBsum; 5M0X; -.
PDBsum; 5M12; -.
PDBsum; 5M16; -.
PDBsum; 5M1I; -.
PDBsum; 6GTA; -.
PDBsum; 6GVD; -.
PDBsum; 6GWF; -.
PDBsum; 6GWG; -.
PDBsum; 6GX8; -.
ProteinModelPortal; G4FEF4; -.
SMR; G4FEF4; -.
STRING; 243274.TM1192; -.
ChEMBL; CHEMBL3308963; -.
CAZy; GH36; Glycoside Hydrolase Family 36.
DNASU; 898292; -.
EnsemblBacteria; AAD36267; AAD36267; TM_1192.
EnsemblBacteria; AGL50123; AGL50123; Tmari_1199.
GeneID; 898292; -.
KEGG; tma:TM1192; -.
KEGG; tmi:THEMA_08370; -.
KEGG; tmm:Tmari_1199; -.
KEGG; tmw:THMA_1218; -.
PATRIC; fig|243274.17.peg.1197; -.
eggNOG; ENOG4107R49; Bacteria.
eggNOG; COG3345; LUCA.
InParanoid; G4FEF4; -.
KO; K07407; -.
OMA; ILGCGAP; -.
BioCyc; TMAR243274:G1H0Q-1680-MONOMER; -.
BRENDA; 3.2.1.22; 6331.
Proteomes; UP000008183; Chromosome.
Proteomes; UP000013901; Chromosome.
GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0016139; P:glycoside catabolic process; IDA:UniProtKB.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR011013; Gal_mutarotase_sf_dom.
InterPro; IPR002252; Glyco_hydro_36.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF02065; Melibiase; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF74650; SSF74650; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Complete proteome;
Direct protein sequencing; Glycosidase; Hydrolase; Reference proteome.
CHAIN 1 552 Alpha-galactosidase.
/FTId=PRO_0000439021.
REGION 220 221 Substrate binding. {ECO:0000244|PDB:5M16,
ECO:0000269|PubMed:27783466}.
REGION 325 327 Substrate binding. {ECO:0000244|PDB:5M16,
ECO:0000269|PubMed:27783466}.
ACT_SITE 327 327 Nucleophile.
{ECO:0000269|PubMed:17323919}.
ACT_SITE 387 387 Proton donor/acceptor.
{ECO:0000269|PubMed:17323919}.
BINDING 65 65 Substrate. {ECO:0000244|PDB:5M16,
ECO:0000269|PubMed:27783466}.
BINDING 191 191 Substrate. {ECO:0000244|PDB:5M16,
ECO:0000269|PubMed:27783466}.
BINDING 368 368 Substrate. {ECO:0000244|PDB:5M16,
ECO:0000269|PubMed:27783466}.
BINDING 383 383 Substrate. {ECO:0000244|PDB:5M16,
ECO:0000269|PubMed:27783466}.
MUTAGEN 220 220 D->A: Less than 1% of the wild-type
enzyme activity with p-nitrophenyl-alpha-
D-galactopyranoside as substrate at 80
degrees Celsius.
{ECO:0000269|PubMed:17323919}.
MUTAGEN 220 220 D->G: Reduced activity compared to the
wild-type enzyme.
{ECO:0000269|PubMed:17323919}.
MUTAGEN 327 327 D->A: Less than 1% of the wild-type
enzyme activity with p-nitrophenyl-alpha-
D-galactopyranoside as substrate at 80
degrees Celsius.
{ECO:0000269|PubMed:17323919}.
MUTAGEN 327 327 D->G: Between 200 and 800-fold lower
catalytic rate and between 300 and 1700-
fold lower catalytic efficiency than the
wild-type enzyme with aryl-alpha-
galactosides as substrates.
{ECO:0000269|PubMed:17323919}.
MUTAGEN 328 328 F->A: Increased transglycosylating
activity at high concentrations of p-
nitrophenyl-alpha-D-galactopyranoside
substrate, which could be useful in
industry and medicine for the synthesis
of different p-nitrophenyl-
digalactosides. Able to produce 16 times
more of a regio-isomer with the
(alpha1,2)-bond than wild-type enzyme.
{ECO:0000269|PubMed:24237145}.
MUTAGEN 385 385 G->L: Increased transglycosylating
activity at high concentrations of p-
nitrophenyl-alpha-D-galactopyranoside
substrate, which could be useful in
industry and medicine for the synthesis
of different p-nitrophenyl-
digalactosides.
{ECO:0000269|PubMed:24237145}.
MUTAGEN 387 387 D->A: Less than 1% of the wild-type
enzyme activity with p-nitrophenyl-alpha-
D-galactopyranoside as substrate at 80
degrees Celsius.
{ECO:0000269|PubMed:17323919}.
MUTAGEN 387 387 D->G: 1500-fold lower catalytic rate and
1000-fold lower catalytic efficiency than
the wild-type enzyme with p-nitrophenyl-
alpha-D-galactopyranoside as substrate.
{ECO:0000269|PubMed:17323919}.
MUTAGEN 402 402 P->D: Increased transglycosylating
activity at high concentrations of p-
nitrophenyl-alpha-D-galactopyranoside
substrate, which could be useful in
industry and medicine for the synthesis
of different p-nitrophenyl-
digalactosides.
{ECO:0000269|PubMed:24237145}.
STRAND 1 3 {ECO:0000244|PDB:1ZY9}.
STRAND 10 16 {ECO:0000244|PDB:6GVD}.
STRAND 18 29 {ECO:0000244|PDB:6GVD}.
STRAND 32 41 {ECO:0000244|PDB:6GVD}.
STRAND 45 52 {ECO:0000244|PDB:6GVD}.
STRAND 55 60 {ECO:0000244|PDB:6GVD}.
STRAND 68 75 {ECO:0000244|PDB:6GVD}.
HELIX 83 85 {ECO:0000244|PDB:1ZY9}.
HELIX 86 89 {ECO:0000244|PDB:6GVD}.
HELIX 93 96 {ECO:0000244|PDB:6GVD}.
STRAND 101 108 {ECO:0000244|PDB:6GVD}.
STRAND 111 116 {ECO:0000244|PDB:6GVD}.
STRAND 119 128 {ECO:0000244|PDB:6GVD}.
STRAND 131 137 {ECO:0000244|PDB:6GVD}.
STRAND 143 148 {ECO:0000244|PDB:6GVD}.
STRAND 152 156 {ECO:0000244|PDB:6GVD}.
HELIX 160 175 {ECO:0000244|PDB:6GVD}.
STRAND 185 189 {ECO:0000244|PDB:6GVD}.
HELIX 190 193 {ECO:0000244|PDB:6GVD}.
HELIX 194 196 {ECO:0000244|PDB:6GVD}.
HELIX 199 208 {ECO:0000244|PDB:6GVD}.
HELIX 209 211 {ECO:0000244|PDB:6GVD}.
STRAND 215 219 {ECO:0000244|PDB:6GVD}.
STRAND 223 226 {ECO:0000244|PDB:6GVD}.
HELIX 240 249 {ECO:0000244|PDB:6GVD}.
STRAND 253 258 {ECO:0000244|PDB:6GVD}.
STRAND 262 264 {ECO:0000244|PDB:6GVD}.
HELIX 268 272 {ECO:0000244|PDB:6GVD}.
HELIX 274 276 {ECO:0000244|PDB:6GVD}.
STRAND 286 290 {ECO:0000244|PDB:6GVD}.
STRAND 293 298 {ECO:0000244|PDB:6GVD}.
HELIX 303 319 {ECO:0000244|PDB:6GVD}.
STRAND 323 326 {ECO:0000244|PDB:6GVD}.
HELIX 329 333 {ECO:0000244|PDB:6GVD}.
STRAND 335 337 {ECO:0000244|PDB:6GVD}.
STRAND 339 341 {ECO:0000244|PDB:6GVD}.
HELIX 344 359 {ECO:0000244|PDB:6GVD}.
STRAND 363 367 {ECO:0000244|PDB:6GVD}.
HELIX 373 375 {ECO:0000244|PDB:6GVD}.
TURN 376 378 {ECO:0000244|PDB:6GVD}.
STRAND 380 383 {ECO:0000244|PDB:6GVD}.
STRAND 398 401 {ECO:0000244|PDB:6GVD}.
HELIX 404 413 {ECO:0000244|PDB:6GVD}.
HELIX 415 417 {ECO:0000244|PDB:6GVD}.
TURN 418 420 {ECO:0000244|PDB:6GVD}.
STRAND 421 425 {ECO:0000244|PDB:6GVD}.
STRAND 433 435 {ECO:0000244|PDB:6GVD}.
HELIX 440 452 {ECO:0000244|PDB:6GVD}.
STRAND 457 459 {ECO:0000244|PDB:6GVD}.
HELIX 463 465 {ECO:0000244|PDB:6GVD}.
HELIX 468 478 {ECO:0000244|PDB:6GVD}.
STRAND 482 487 {ECO:0000244|PDB:6GVD}.
TURN 488 491 {ECO:0000244|PDB:6GVD}.
STRAND 493 504 {ECO:0000244|PDB:6GVD}.
STRAND 507 514 {ECO:0000244|PDB:6GVD}.
TURN 515 518 {ECO:0000244|PDB:6GVD}.
STRAND 519 524 {ECO:0000244|PDB:6GVD}.
SEQUENCE 552 AA; 63657 MW; 91C6E6EFA24EA9D5 CRC64;
MEIFGKTFRE GRFVLKEKNF TVEFAVEKIH LGWKISGRVK GSPGRLEVLR TKAPEKVLVN
NWQSWGPCRV VDAFSFKPPE IDPNWRYTAS VVPDVLERNL QSDYFVAEEG KVYGFLSSKI
AHPFFAVEDG ELVAYLEYFD VEFDDFVPLE PLVVLEDPNT PLLLEKYAEL VGMENNARVP
KHTPTGWCSW YHYFLDLTWE ETLKNLKLAK NFPFEVFQID DAYEKDIGDW LVTRGDFPSV
EEMAKVIAEN GFIPGIWTAP FSVSETSDVF NEHPDWVVKE NGEPKMAYRN WNKKIYALDL
SKDEVLNWLF DLFSSLRKMG YRYFKIDFLF AGAVPGERKK NITPIQAFRK GIETIRKAVG
EDSFILGCGS PLLPAVGCVD GMRIGPDTAP FWGEHIEDNG APAARWALRN AITRYFMHDR
FWLNDPDCLI LREEKTDLTQ KEKELYSYTC GVLDNMIIES DDLSLVRDHG KKVLKETLEL
LGGRPRVQNI MSEDLRYEIV SSGTLSGNVK IVVDLNSREY HLEKEGKSSL KKRVVKREDG
RNFYFYEEGE RE


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18-272-196702 beta Galactosidase - Rabbit polyclonal to beta Galactosidase; EC 3.4.16.5; Cathepsin A; Carboxypeptidase C; Protective protein for beta-galactosidase Polyclonal 0.1 mg
20-272-190060 beta Galactosidase - Mouse monoclonal [2E9] to beta Galactosidase; EC 3.4.16.5; Cathepsin A; Carboxypeptidase C; Protective protein for beta-galactosidase Monoclonal 0.1 mg
20-272-192185 beta Galactosidase - Mouse monoclonal [BG - 02] to beta Galactosidase; EC 3.4.16.5; Cathepsin A; Carboxypeptidase C; Protective protein for beta-galactosidase Monoclonal 0.1 mg
20-272-191989 beta Galactosidase - Mouse monoclonal [DC1 4C7] to beta Galactosidase; EC 3.4.16.5; Cathepsin A; Carboxypeptidase C; Protective protein for beta-galactosidase Monoclonal 0.1 mg
YF-PA12024 anti-Galactosidase alpha 50 ug
enz-609 Recombinant E.Coli Alpha-Galactosidase 10
EH745 Alpha-galactosidase A Elisa Kit 96T
E90183Hu ELISA Kit for Galactosidase, Alpha (GLa) 96T/Kit
REN-609 Recombinant E.Coli Alpha-Galactosidase 2


 

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