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Galactose oxidase (GAO) (GO) (GOase) (EC 1.1.3.9)

 GAOA_GIBZA              Reviewed;         680 AA.
P0CS93; O43098; Q01745; Q4HVH6;
11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
11-JUL-2012, sequence version 1.
27-SEP-2017, entry version 25.
RecName: Full=Galactose oxidase;
Short=GAO;
Short=GO;
Short=GOase;
EC=1.1.3.9;
Flags: Precursor;
Name=GAOA;
Gibberella zeae (Wheat head blight fungus) (Fusarium graminearum).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
Fusarium.
NCBI_TaxID=5518;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 46032 / CBS 110244 / NRRL 2903;
PubMed=1569070;
McPherson M.J., Ogel Z.B., Stevens C.E., Yadav K.D.S., Keen J.N.,
Knowles P.F.;
"Galactose oxidase of Dactylium dendroides. Gene cloning and sequence
analysis.";
J. Biol. Chem. 267:8146-8152(1992).
[2]
PROTEIN SEQUENCE OF 25-33 AND 42-50, AND PROPEPTIDE CLEAVAGE.
STRAIN=ATCC 46032 / CBS 110244 / NRRL 2903;
DOI=10.1021/ja993385y;
Rogers M.S., Baron A.J., McPherson M.J., Knowles P.F., Dooley D.M.;
"Galactose oxidase pro-sequence cleavage and cofactor assembly are
self-processing reactions.";
J. Am. Chem. Soc. 122:990-991(2000).
[3]
PROTEIN SEQUENCE OF 42-47, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF ARG-371 AND PHE-505.
PubMed=15239055; DOI=10.1002/cbic.200300810;
Deacon S.E., Mahmoud K., Spooner R.K., Firbank S.J., Knowles P.F.,
Phillips S.E., McPherson M.J.;
"Enhanced fructose oxidase activity in a galactose oxidase variant.";
ChemBioChem 5:972-979(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-142.
STRAIN=DSM 4527 / 183;
DOI=10.1016/S0723-2020(97)80055-0;
Niessen M.L., Vogel R.F.;
"Specific identification of Fusarium graminearum by PCR with gaoA
targeted primers.";
Syst. Appl. Microbiol. 20:111-123(1997).
[5]
FUNCTION.
PubMed=13641238;
Cooper J.A., Smith W., Bacila M., Medina H.;
"Galactose oxidase from Polyporus circinatus, Fr.";
J. Biol. Chem. 234:445-448(1959).
[6]
SUBSTRATE SPECIFICITY.
PubMed=13863403;
Avigad G., Amaral D., Asensio C., Horecker B.L.;
"The D-galactose oxidase of Polyporus circinatus.";
J. Biol. Chem. 237:2736-2743(1962).
[7]
TAXONOMY.
DOI=10.1016/0006-291X(63)90251-1;
Nobles M.K., Madhosingh C.;
"Dactylium dendroides (Bull.) Fr. misnamed as Polyporus circinatus
Fr.";
Biochem. Biophys. Res. Commun. 12:146-147(1963).
[8]
ENZYME REGULATION, AND COPPER-BINDING.
PubMed=14012475;
Amaral D., Bernstein L., Morse D., Horecker B.L.;
"Galactose oxidase of Polyporus circinatus: a copper enzyme.";
J. Biol. Chem. 238:2281-2284(1963).
[9]
FUNCTION, AND SUBUNIT.
PubMed=4441089; DOI=10.1016/0003-9861(74)90271-9;
Kosman D.J., Ettinger M.J., Weiner R.E., Massaro E.J.;
"The molecular properties of the copper enzyme galactose oxidase.";
Arch. Biochem. Biophys. 165:456-467(1974).
[10]
TAXONOMY.
AGRICOLA=IND20498749;
Ogel Z.B., Brayford D., McPherson M.J.;
"Cellulose-triggered sporulation in the galactose oxidase producing
fungus Cladobotryum (Dactylium) dendroides NRRL 2903 and its re-
identification as a species of Fusarium.";
Mycol. Res. 98:474-480(1994).
[11]
REACTION MECHANISM.
PubMed=11401560; DOI=10.1021/bi010303l;
Whittaker M.M., Whittaker J.W.;
"Catalytic reaction profile for alcohol oxidation by galactose
oxidase.";
Biochemistry 40:7140-7148(2001).
[12]
PROTEIN MATURATION.
PubMed=12672814; DOI=10.1074/jbc.M300112200;
Whittaker M.M., Whittaker J.W.;
"Cu(I)-dependent biogenesis of the galactose oxidase redox cofactor.";
J. Biol. Chem. 278:22090-22101(2003).
[13]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 42-680 IN COMPLEX WITH COPPER
IONS.
PubMed=2002850; DOI=10.1038/350087a0;
Ito N., Phillips S.E.V., Stevens C.E., Ogel Z.B., McPherson M.J.,
Keen J.N., Yadav K.D.S., Knowles P.F.;
"Novel thioether bond revealed by a 1.7 A crystal structure of
galactose oxidase.";
Nature 350:87-90(1991).
[14]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-680 OF MUTANTS GLY-269 AND
HIS-331 IN COMPLEX WITH COPPER IONS, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=7929198;
Baron A.J., Stevens C., Wilmot C., Seneviratne K.D., Blakeley V.,
Dooley D.M., Phillips S.E., Knowles P.F., McPherson M.J.;
"Structure and mechanism of galactose oxidase. The free radical
site.";
J. Biol. Chem. 269:25095-25105(1994).
[15]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 42-680 OF MUTANT PHE-536 IN
COMPLEX WITH COPPER IONS, ACTIVE SITE, AND BIOPHYSICOCHEMICAL
PROPERTIES.
DOI=10.1007/s007750050139;
Reynolds M.P., Baron A.J., Wilmot C.M., Vinecombe E., Stevens C.,
Phillips S.E.V., Knowles P.F., McPherson M.J.;
"Structure and mechanism of galactose oxidase: catalytic role of
tyrosine 495.";
J. Biol. Inorg. Chem. 2:327-335(1997).
[16]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 25-680.
PubMed=11698678; DOI=10.1073/pnas.231463798;
Firbank S.J., Rogers M.S., Wilmot C.M., Dooley D.M., Halcrow M.A.,
Knowles P.F., McPherson M.J., Phillips S.E.;
"Crystal structure of the precursor of galactose oxidase: an unusual
self-processing enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 98:12932-12937(2001).
[17]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 42-680 OF MUTANT SER-424 IN
COMPLEX WITH COPPER IONS, MASS SPECTROMETRY, MUTAGENESIS OF CYS-424;
TYR-477 AND VAL-535, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 46032 / CBS 110244 / NRRL 2903;
PubMed=15047910; DOI=10.1093/protein/gzh018;
Wilkinson D., Akumanyi N., Hurtado-Guerrero R., Dawkes H.,
Knowles P.F., Phillips S.E.V., McPherson M.J.;
"Structural and kinetic studies of a series of mutants of galactose
oxidase identified by directed evolution.";
Protein Eng. Des. Sel. 17:141-148(2004).
[18]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 42-680 OF MUTANTS GLY-331;
HIS-331 AND PHE-331 IN COMPLEX WITH COPPER IONS, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17385891; DOI=10.1021/bi062139d;
Rogers M.S., Tyler E.M., Akyumani N., Kurtis C.R., Spooner R.K.,
Deacon S.E., Tamber S., Firbank S.J., Mahmoud K., Knowles P.F.,
Phillips S.E.V., McPherson M.J., Dooley D.M.;
"The stacking tryptophan of galactose oxidase: a second-coordination
sphere residue that has profound effects on tyrosyl radical behavior
and enzyme catalysis.";
Biochemistry 46:4606-4618(2007).
-!- FUNCTION: Catalyzes the sterospecific oxidation of primary
alcohols to the corresponding aldehydes. The biologically relevant
substrate of the enzyme is not known as the enzyme exhibits broad
substrate specificity from small alcohols through sugars to
oligo- and polysaccharides. {ECO:0000269|PubMed:13641238,
ECO:0000269|PubMed:4441089}.
-!- CATALYTIC ACTIVITY: D-galactose + O(2) = D-galacto-hexodialdose +
H(2)O(2).
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Note=Binds 1 Cu(2+) ion per subunit.;
-!- ENZYME REGULATION: Inhibited by diethyldithiocarbamate.
{ECO:0000269|PubMed:14012475}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=56 mM for 1-methyl-alpha-D-galactopyranoside
{ECO:0000269|PubMed:15047910, ECO:0000269|PubMed:15239055,
ECO:0000269|PubMed:17385891, ECO:0000269|PubMed:7929198,
ECO:0000269|Ref.15};
KM=57 mM for 2-methylene-1,3-propanediol
{ECO:0000269|PubMed:15047910, ECO:0000269|PubMed:15239055,
ECO:0000269|PubMed:17385891, ECO:0000269|PubMed:7929198,
ECO:0000269|Ref.15};
KM=68 mM for D-galactose {ECO:0000269|PubMed:15047910,
ECO:0000269|PubMed:15239055, ECO:0000269|PubMed:17385891,
ECO:0000269|PubMed:7929198, ECO:0000269|Ref.15};
KM=2.5 M for D-fructose {ECO:0000269|PubMed:15047910,
ECO:0000269|PubMed:15239055, ECO:0000269|PubMed:17385891,
ECO:0000269|PubMed:7929198, ECO:0000269|Ref.15};
pH dependence:
Optimum pH is 7. Active from pH 5.7 to 9.4.
{ECO:0000269|PubMed:15047910, ECO:0000269|PubMed:15239055,
ECO:0000269|PubMed:17385891, ECO:0000269|PubMed:7929198,
ECO:0000269|Ref.15};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15047910,
ECO:0000269|PubMed:17385891, ECO:0000269|PubMed:2002850,
ECO:0000269|PubMed:4441089, ECO:0000269|PubMed:7929198,
ECO:0000269|Ref.15}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: Galactose oxidase contains a protein-derived free radical
cofactor. In the active state, Tyr-313, which is cross-linked to
Cys-269 via a thioether bond, is oxidized to a radical and acts
with Cu(2+) as a two-electron acceptor in the oxidation reaction.
The cross-link is believed to modulate the redox potential of the
tyrosyl radical, which is further stabilized by a stacking
interaction with Trp-331 in the active site. The post-
translational formation of the cross-link is closely linked to the
propeptide cleavage event, and both are copper-dependent,
autocatalytic processes. The propeptide may act as an
intramolecular chaperone, facilitating thioester bond formation
and copper binding by positioning of active-site residues,
including copper ligands.
-!- MASS SPECTROMETRY: Mass=68520; Method=Electrospray; Range=42-680;
Evidence={ECO:0000269|PubMed:15047910};
-!- CAUTION: Was originally thought to originate from Polyporus
circinatus then later from Dactylium dendroides and is now known
to be originating from Gibberella (Fusarium). {ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/GAO/";
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EMBL; M86819; AAA16228.1; -; Unassigned_DNA.
EMBL; AH005781; AAB94635.1; -; Genomic_DNA.
PDB; 1GOF; X-ray; 1.70 A; A=42-680.
PDB; 1GOG; X-ray; 1.90 A; A=42-680.
PDB; 1GOH; X-ray; 2.20 A; A=42-680.
PDB; 1K3I; X-ray; 1.40 A; A=25-680.
PDB; 1T2X; X-ray; 2.30 A; A=42-680.
PDB; 2EIB; X-ray; 2.10 A; A=42-680.
PDB; 2EIC; X-ray; 2.80 A; A=42-680.
PDB; 2EID; X-ray; 2.20 A; A=42-680.
PDB; 2EIE; X-ray; 1.80 A; A=42-680.
PDB; 2JKX; X-ray; 1.84 A; A=42-680.
PDB; 2VZ1; X-ray; 1.91 A; A=42-680.
PDB; 2VZ3; X-ray; 1.90 A; A=42-680.
PDB; 2WQ8; X-ray; 2.19 A; A=42-680.
PDBsum; 1GOF; -.
PDBsum; 1GOG; -.
PDBsum; 1GOH; -.
PDBsum; 1K3I; -.
PDBsum; 1T2X; -.
PDBsum; 2EIB; -.
PDBsum; 2EIC; -.
PDBsum; 2EID; -.
PDBsum; 2EIE; -.
PDBsum; 2JKX; -.
PDBsum; 2VZ1; -.
PDBsum; 2VZ3; -.
PDBsum; 2WQ8; -.
ProteinModelPortal; P0CS93; -.
SMR; P0CS93; -.
CAZy; AA5; Auxiliary Activities 5.
CAZy; CBM32; Carbohydrate-Binding Module Family 32.
eggNOG; ENOG410IJM5; Eukaryota.
eggNOG; ENOG410XSZ3; LUCA.
BioCyc; MetaCyc:MONOMER-15357; -.
SABIO-RK; P0CS93; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0045480; F:galactose oxidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
CDD; cd02851; E_set_GO_C; 1.
Gene3D; 2.130.10.80; -; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR000421; FA58C.
InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
InterPro; IPR015916; Gal_Oxidase_b-propeller.
InterPro; IPR008979; Galactose-bd-like.
InterPro; IPR015202; GO-like_E_set.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR006652; Kelch_1.
Pfam; PF09118; DUF1929; 1.
Pfam; PF00754; F5_F8_type_C; 1.
Pfam; PF01344; Kelch_1; 1.
SMART; SM00231; FA58C; 1.
SMART; SM00612; Kelch; 3.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF50965; SSF50965; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50022; FA58C_3; 1.
1: Evidence at protein level;
3D-structure; Copper; Direct protein sequencing; Disulfide bond;
Kelch repeat; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal;
Thioether bond.
SIGNAL 1 24 {ECO:0000269|Ref.2}.
PROPEP 25 41 {ECO:0000269|PubMed:15239055,
ECO:0000269|Ref.2}.
/FTId=PRO_0000285407.
CHAIN 42 680 Galactose oxidase.
/FTId=PRO_0000016610.
DOMAIN 42 189 F5/8 type C. {ECO:0000255|PROSITE-
ProRule:PRU00081}.
REPEAT 223 268 Kelch 1.
REPEAT 279 321 Kelch 2.
REPEAT 323 372 Kelch 3.
REPEAT 436 490 Kelch 4.
REPEAT 492 544 Kelch 5.
ACT_SITE 536 536 Proton acceptor. {ECO:0000269|Ref.15}.
METAL 313 313 Copper.
METAL 536 536 Copper.
METAL 537 537 Copper.
METAL 622 622 Copper.
DISULFID 59 68
DISULFID 556 559
CROSSLNK 269 313 3'-(S-cysteinyl)-tyrosine (Cys-Tyr).
MUTAGEN 269 269 C->G: Reduces catalytic activity more
than 10000-fold.
MUTAGEN 331 331 W->F: Reduces catalytic efficiency 50-
fold and substrate affinity 36-fold.
MUTAGEN 331 331 W->G: Reduces substrate affinity 20-fold
and catalytic activity more than 6000-
fold.
MUTAGEN 331 331 W->H: Reduces catalytic efficiency 1000-
fold.
MUTAGEN 371 371 R->A: Reduces catalytic efficiency 250-
fold and substrate affinity 22-fold for
D-galactose, but improves catalytic
efficiency 1.8-fold towards D-fructose.
{ECO:0000269|PubMed:15239055}.
MUTAGEN 371 371 R->K: Reduces catalytic efficiency 45-
fold and substrate affinity 8.7-fold for
D-galactose, but improves catalytic
efficiency 8-fold towards D-fructose.
{ECO:0000269|PubMed:15239055}.
MUTAGEN 424 424 C->A: Reduces catalytic efficiency 1.5-to
2-fold towards D-galactose and 1-methyl-
alpha-D-galactopyranoside.
{ECO:0000269|PubMed:15047910}.
MUTAGEN 424 424 C->S: Improves catalytic efficiency 3- to
4-fold towards D-galactose and 1-methyl-
alpha-D-galactopyranoside, mainly by
increasing the affinity for the
substrates. Improves catalytic efficiency
5.3-fold towards D-galactose; when
associated with H-477. Improves catalytic
efficiency 4.9-fold towards 1-methyl-
alpha-D-galactopyranoside; when
associated with A-535. Improves catalytic
activity 4.7-fold towards D-galactose,
but only 1.8-fold towards 1-methyl-alpha-
D-galactopyranoside; when associated with
A-477. {ECO:0000269|PubMed:15047910}.
MUTAGEN 477 477 Y->A: No effect. Improves catalytic
efficiency 2- to 3-fold towards D-
galactose and 1-methyl-alpha-D-
galactopyranoside; when associated with
A-535. Improves catalytic activity 4.7-
fold towards D-galactose, but only 1.8-
fold towards 1-methyl-alpha-D-
galactopyranoside; when associated with
S-424. {ECO:0000269|PubMed:15047910}.
MUTAGEN 477 477 Y->H: No effect. Improves catalytic
efficiency 5.3-fold towards D-galactose;
when associated with S-424.
{ECO:0000269|PubMed:15047910}.
MUTAGEN 505 505 F->A: Reduces catalytic efficiency 166-
fold and substrate affinity 9-fold.
{ECO:0000269|PubMed:15239055}.
MUTAGEN 535 535 V->A: Improves catalytic efficiency 1.3-
to 1.8-fold. Improves catalytic
efficiency 2- to 3-fold towards D-
galactose and 1-methyl-alpha-D-
galactopyranoside; when associated with
A-477. Improves catalytic efficiency 4.9-
fold towards 1-methyl-alpha-D-
galactopyranoside; when associated with
S-424. {ECO:0000269|PubMed:15047910}.
MUTAGEN 536 536 Y->F: Reduces catalytic efficiency 1000-
fold, but does not reduce substrate
affinity.
CONFLICT 111 111 M -> I (in Ref. 4; AAB94635).
{ECO:0000305}.
HELIX 35 37 {ECO:0000244|PDB:1K3I}.
STRAND 46 49 {ECO:0000244|PDB:1K3I}.
STRAND 56 60 {ECO:0000244|PDB:1K3I}.
HELIX 68 71 {ECO:0000244|PDB:1K3I}.
STRAND 72 74 {ECO:0000244|PDB:1K3I}.
HELIX 85 87 {ECO:0000244|PDB:1K3I}.
STRAND 94 112 {ECO:0000244|PDB:1K3I}.
STRAND 125 135 {ECO:0000244|PDB:1K3I}.
STRAND 141 145 {ECO:0000244|PDB:1K3I}.
STRAND 148 151 {ECO:0000244|PDB:1K3I}.
STRAND 153 169 {ECO:0000244|PDB:1K3I}.
STRAND 180 188 {ECO:0000244|PDB:1K3I}.
STRAND 201 207 {ECO:0000244|PDB:1K3I}.
STRAND 213 217 {ECO:0000244|PDB:1K3I}.
TURN 219 221 {ECO:0000244|PDB:1K3I}.
STRAND 224 229 {ECO:0000244|PDB:1K3I}.
TURN 233 235 {ECO:0000244|PDB:1K3I}.
STRAND 241 248 {ECO:0000244|PDB:1K3I}.
TURN 250 252 {ECO:0000244|PDB:1K3I}.
STRAND 259 262 {ECO:0000244|PDB:1K3I}.
STRAND 271 274 {ECO:0000244|PDB:1K3I}.
STRAND 280 283 {ECO:0000244|PDB:1K3I}.
STRAND 285 287 {ECO:0000244|PDB:1K3I}.
STRAND 291 295 {ECO:0000244|PDB:1K3I}.
TURN 296 299 {ECO:0000244|PDB:1K3I}.
STRAND 300 303 {ECO:0000244|PDB:1K3I}.
STRAND 315 318 {ECO:0000244|PDB:1K3I}.
STRAND 324 327 {ECO:0000244|PDB:1K3I}.
STRAND 333 335 {ECO:0000244|PDB:1K3I}.
STRAND 340 344 {ECO:0000244|PDB:1K3I}.
TURN 345 348 {ECO:0000244|PDB:1K3I}.
STRAND 349 353 {ECO:0000244|PDB:1K3I}.
HELIX 359 361 {ECO:0000244|PDB:1K3I}.
HELIX 368 370 {ECO:0000244|PDB:1K3I}.
TURN 371 373 {ECO:0000244|PDB:1K3I}.
STRAND 378 380 {ECO:0000244|PDB:1K3I}.
HELIX 382 384 {ECO:0000244|PDB:1K3I}.
STRAND 386 388 {ECO:0000244|PDB:1K3I}.
STRAND 391 399 {ECO:0000244|PDB:1K3I}.
STRAND 405 411 {ECO:0000244|PDB:1K3I}.
STRAND 426 431 {ECO:0000244|PDB:1K3I}.
TURN 432 435 {ECO:0000244|PDB:1K3I}.
STRAND 436 440 {ECO:0000244|PDB:1K3I}.
STRAND 443 450 {ECO:0000244|PDB:1K3I}.
STRAND 455 459 {ECO:0000244|PDB:1K3I}.
STRAND 468 471 {ECO:0000244|PDB:1K3I}.
STRAND 480 482 {ECO:0000244|PDB:1GOH}.
STRAND 484 487 {ECO:0000244|PDB:1K3I}.
STRAND 493 496 {ECO:0000244|PDB:1K3I}.
STRAND 499 501 {ECO:0000244|PDB:1K3I}.
STRAND 515 518 {ECO:0000244|PDB:1K3I}.
HELIX 519 521 {ECO:0000244|PDB:1K3I}.
STRAND 523 526 {ECO:0000244|PDB:1K3I}.
STRAND 538 542 {ECO:0000244|PDB:1K3I}.
STRAND 548 552 {ECO:0000244|PDB:1K3I}.
STRAND 565 570 {ECO:0000244|PDB:1K3I}.
HELIX 572 574 {ECO:0000244|PDB:1K3I}.
STRAND 579 581 {ECO:0000244|PDB:1K3I}.
STRAND 587 591 {ECO:0000244|PDB:1K3I}.
STRAND 593 596 {ECO:0000244|PDB:1K3I}.
STRAND 600 607 {ECO:0000244|PDB:1K3I}.
STRAND 610 616 {ECO:0000244|PDB:1K3I}.
STRAND 619 621 {ECO:0000244|PDB:1K3I}.
STRAND 630 632 {ECO:0000244|PDB:1K3I}.
STRAND 635 639 {ECO:0000244|PDB:1K3I}.
STRAND 642 646 {ECO:0000244|PDB:1K3I}.
TURN 651 653 {ECO:0000244|PDB:1K3I}.
STRAND 656 664 {ECO:0000244|PDB:1K3I}.
STRAND 674 679 {ECO:0000244|PDB:1K3I}.
SEQUENCE 680 AA; 72823 MW; 2F97C561B63E46E9 CRC64;
MKHLLTLALC FSSINAVAVT VPHKAVGTGI PEGSLQFLSL RASAPIGSAI SRNNWAVTCD
SAQSGNECNK AIDGNKDTFW HTFYGANGDP KPPHTYTIDM KTTQNVNGLS MLPRQDGNQN
GWIGRHEVYL SSDGTNWGSP VASGSWFADS TTKYSNFETR PARYVRLVAI TEANGQPWTS
IAEINVFQAS SYTAPQPGLG RWGPTIDLPI VPAAAAIEPT SGRVLMWSSY RNDAFGGSPG
GITLTSSWDP STGIVSDRTV TVTKHDMFCP GISMDGNGQI VVTGGNDAKK TSLYDSSSDS
WIPGPDMQVA RGYQSSATMS DGRVFTIGGS WSGGVFEKNG EVYSPSSKTW TSLPNAKVNP
MLTADKQGLY RSDNHAWLFG WKKGSVFQAG PSTAMNWYYT SGSGDVKSAG KRQSNRGVAP
DAMCGNAVMY DAVKGKILTF GGSPDYQDSD ATTNAHIITL GEPGTSPNTV FASNGLYFAR
TFHTSVVLPD GSTFITGGQR RGIPFEDSTP VFTPEIYVPE QDTFYKQNPN SIVRVYHSIS
LLLPDGRVFN GGGGLCGDCT TNHFDAQIFT PNYLYNSNGN LATRPKITRT STQSVKVGGR
ITISTDSSIS KASLIRYGTA THTVNTDQRR IPLTLTNNGG NSYSFQVPSD SGVALPGYWM
LFVMNSAGVP SVASTIRVTQ


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9028-79-9 Galactose oxidase Galactose oxidase 1g
26-502 B3GALT6 (Beta-1,3-galactosyltransferase) transfers galactose from UDP-galactose to substrates with a terminal beta-linked galactose residue. It has a preference for galactose-beta-1,4-xylose that is f 0.05 mg
GLS004522 Galactose oxidase 450 U
GLS004520 Galactose oxidase 150U
G00260 Galactose Oxidase 1000 UN
GLS004524 Galactose oxidase 1 KU
G00260 Galactose Oxidase 10000 UN
GLS004524 Galactose oxidase 1 KU
GLS004520 Galactose oxidase 150U
GLS004522 Galactose oxidase 450 U
G00260 Galactose oxidase 3KU per gram 1000 UN
G00260 Galactose oxidase 3KU per gram 10000 UN
30-412 Galactose-1-phosphate uridyl transferase (GALT) catalyzes the second step of the Leloir pathway of galactose metabolism, namely the conversion of UDP-glucose + galactose-1-phosphate to glucose-1-phosp 0.05 mg
B1104 Phenol Red Galactose Broth USE For Galactose fermentation studies of microorganisms. Qty per Litre of Medium: 21
B1104 Phenol Red Galactose Broth USE : For Galactose fermentation studies of microorganisms. 5x500gm
EGAL-100 EnzyChrom™ Galactose Assay Kit, Quantitative determination of galactose by colorimetric (570nm) or fluorimetric (530nm_590nm) methods 100Tests
EIAAB36890 Bos taurus,Bovine,SLC35A2,Solute carrier family 35 member A2,UDP-galactose translocator,UDP-galactose transporter,UDP-Gal-Tr,UGT
EIAAB36891 Mouse,mUGT1,Mus musculus,Slc35a2,Solute carrier family 35 member A2,UDP-galactose translocator,UDP-galactose transporter,UDP-Gal-Tr,UGT,Ugt1
26-670 GALM is an enzyme that catalyzes the epimerization of hexose sugars such as glucose and galactose. It is expressed in the cytoplasm and has a preference for galactose. The protein may be required for 0.05 mg
30-578 GAL3ST3 is a member of the galactose-3-O-sulfotransferase protein family. It catalyzes sulfonation by transferring a sulfate group to the 3' position of galactose in N-acetyllactosamine in both type 2 0.05 mg
EIAAB36892 Homo sapiens,Human,SLC35A2,Solute carrier family 35 member A2,UDP-galactose translocator,UDP-galactose transporter,UDP-Gal-Tr,UGALT,UGT,UGT,UGTL
26-481 GAL3ST3 is a member of the galactose-3-O-sulfotransferase protein family. It catalyzes sulfonation by transferring a sulfate group to the 3' position of galactose in N-acetyllactosamine in both type 2 0.05 mg
EIAAB36909 Mouse,Mus musculus,Slc35b1,Solute carrier family 35 member B1,UDP-galactose translocator 2,UDP-galactose transporter-related protein 1,Ugalt2,UGTrel1
EGAL-100 EnzyChrom™ Galactose Assay Kit, Quantitative determination of galactose by colorimetric (570nm) or fluorimetric (530nm_590nm) methods. Procedure 20 min. Kit size 100 tests. Detection limit 10 µM. S 100tests
26-862 GALE is an UDP-galactose-4-epimerase which catalyzes two distinct but analogous reactions the epimerization of UDP-glucose to UDP-galactose, and the epimerization of UDP-N-acetylglucosamine to UDP-N- 0.05 mg


 

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