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Myrosinase 1 (EC 3.2.1.147) (Beta-glucosidase 38) (AtBGLU38) (EC 3.2.1.21) (Sinigrinase 1) (Thioglucosidase 1)

 BGL38_ARATH             Reviewed;         541 AA.
P37702; B9DHN6; Q3E942; Q3V5A7; Q3V5A8; Q3V5A9; Q3V5B1; Q3V5B2;
Q3V5B3; Q3V5B4; Q3V5B5; Q3V5B6; Q3V5B7; Q3V5B8; Q3V5B9; Q3V5C0;
Q3V5C2; Q3V5C3; Q3V5C4; Q3V5C5; Q3V5C8; Q3V5D1; Q3V5D2; Q8H7H2;
Q93Z31; Q940N8;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
25-OCT-2017, entry version 146.
RecName: Full=Myrosinase 1;
EC=3.2.1.147;
AltName: Full=Beta-glucosidase 38;
Short=AtBGLU38;
EC=3.2.1.21;
AltName: Full=Sinigrinase 1;
AltName: Full=Thioglucosidase 1;
Flags: Precursor;
Name=TGG1; Synonyms=BGLU38; OrderedLocusNames=At5g26000;
ORFNames=T1N24.7;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=8029343; DOI=10.1104/pp.103.2.671;
Chadchawan S., Bishop J., Thangstad O.P., Bones A.M.,
Mitchell-Olds T., Bradley D.;
"Arabidopsis cDNA sequence encoding myrosinase.";
Plant Physiol. 103:671-671(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=7766881; DOI=10.1007/BF00037019;
Xue J., Joergensen M., Pihlgren U., Rask L.;
"The myrosinase gene family in Arabidopsis thaliana: gene
organization, expression and evolution.";
Plant Mol. Biol. 27:911-922(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-226.
Stracke R., Palme K.;
"Signal peptide selection derived cDNAs from Arabidopsis thaliana
leaves and guard cells.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-497; 43-510; 43-511; 43-512;
43-513; 43-514; 44-511; 44-512; 44-514; 44-522; 45-511 AND 47-512,
FUNCTION, AND VARIANTS ASN-128; LYS-261; GLN-264; ALA-427; GLY-459 AND
ILE-489.
STRAIN=cv. Abd-0, cv. Ag-0, cv. Ba-1, cv. Cal-0, cv. Columbia,
cv. Cvi-0, cv. Db-1, cv. Ei-2, cv. HOG, cv. Ka-0, cv. Ler-1,
cv. Lip-0, cv. Ll-0, cv. Mh-0, cv. Mr-0, cv. Mrk-0, cv. Mt-0,
cv. No-0, cv. Per-1, cv. Petergof, cv. Pi-0, cv. Rsch-0, cv. Sei-0,
cv. Su-0, cv. Ta-0, cv. Tac-0, cv. Tsu-1, and cv. Wl-0;
PubMed=15643972; DOI=10.1111/j.1365-294X.2004.02403.x;
Stranger B.E., Mitchell-Olds T.;
"Nucleotide variation at the myrosinase-encoding locus, TGG1, and
quantitative myrosinase enzyme activity variation in Arabidopsis
thaliana.";
Mol. Ecol. 14:295-309(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-541.
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-250.
STRAIN=cv. C24; TISSUE=Flower bud;
PubMed=8281187; DOI=10.1046/j.1365-313X.1993.04061051.x;
Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P.,
Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R.,
Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y.,
de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M.,
Bardet C., Tremousaygue D., Lescure B.;
"An inventory of 1152 expressed sequence tags obtained by partial
sequencing of cDNAs from Arabidopsis thaliana.";
Plant J. 4:1051-1061(1993).
[10]
TISSUE SPECIFICITY.
PubMed=15316292; DOI=10.1023/B:PLAN.0000038272.99590.10;
Thangstad O.P., Gilde B., Chadchawan S., Seem M., Husebye H.,
Bradley D., Bones A.M.;
"Cell specific, cross-species expression of myrosinases in Brassica
napus, Arabidopsis thaliana and Nicotiana tabacum.";
Plant Mol. Biol. 54:597-611(2004).
[11]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E.,
Esen A.;
"Functional genomic analysis of Arabidopsis thaliana glycoside
hydrolase family 1.";
Plant Mol. Biol. 55:343-367(2004).
[12]
FUNCTION.
PubMed=16640593; DOI=10.1111/j.1365-313X.2006.02716.x;
Barth C., Jander G.;
"Arabidopsis myrosinases TGG1 and TGG2 have redundant function in
glucosinolate breakdown and insect defense.";
Plant J. 46:549-562(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
[14]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19703694; DOI=10.1016/j.phytochem.2009.07.036;
Andersson D., Chakrabarty R., Bejai S., Zhang J., Rask L., Meijer J.;
"Myrosinases from root and leaves of Arabidopsis thaliana have
different catalytic properties.";
Phytochemistry 70:1345-1354(2009).
[15]
FUNCTION.
PubMed=19433491; DOI=10.1093/pcp/pcp066;
Islam M.M., Tani C., Watanabe-Sugimoto M., Uraji M., Jahan M.S.,
Masuda C., Nakamura Y., Mori I.C., Murata Y.;
"Myrosinases, TGG1 and TGG2, redundantly function in ABA and MeJA
signaling in Arabidopsis guard cells.";
Plant Cell Physiol. 50:1171-1175(2009).
-!- FUNCTION: Degradation of glucosinolates (glucose residue linked by
a thioglucoside bound to an amino acid derivative) to glucose,
sulfate and any of the products: thiocyanates, isothiocyanates,
nitriles, epithionitriles or oxazolidine-2-thiones. These toxic
degradation products can deter insect herbivores. Seems to
function in abscisic acid (ABA) and methyl jasmonate (MeJA)
signaling in guard cells. Functionally redundant with TGG2.
Hydrolyzes sinigrin and, with lower efficiency, p-nitrophenyl
beta-D-glucoside. {ECO:0000269|PubMed:15643972,
ECO:0000269|PubMed:16640593, ECO:0000269|PubMed:19433491,
ECO:0000269|PubMed:19703694}.
-!- CATALYTIC ACTIVITY: A thioglucoside + H(2)O = a sugar + a thiol.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-
glucosyl residues with release of beta-D-glucose.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=45 uM for sinigrin (at pH 4.5) {ECO:0000269|PubMed:19703694};
KM=34 mM for p-nitrophenyl beta-D-glucoside (at pH 4.5)
{ECO:0000269|PubMed:19703694};
Vmax=2.3 umol/min/mg enzyme with sinigrin as substrate (at pH
4.5) {ECO:0000269|PubMed:19703694};
Vmax=1.2 umol/min/mg enzyme with p-nitrophenyl beta-D-glucoside
as substrate (at pH 4.5) {ECO:0000269|PubMed:19703694};
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P37702-1; Sequence=Displayed;
Name=2;
IsoId=P37702-2; Sequence=VSP_038446;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Expressed in guard cells, phloem-associated
cells and myrosin cells. {ECO:0000269|PubMed:15316292}.
-!- MISCELLANEOUS: It seems that the absence of a catalytic proton
donor in plant myrosinases is not impairing the hydrolysis of
glucosinolates.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
{ECO:0000305}.
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EMBL; L11454; AAC18869.1; -; mRNA.
EMBL; X79194; CAA55786.1; -; Genomic_DNA.
EMBL; AF149413; AAD40143.1; -; Genomic_DNA.
EMBL; CP002688; AED93511.1; -; Genomic_DNA.
EMBL; CP002688; AED93512.1; -; Genomic_DNA.
EMBL; AY045681; AAK74039.1; -; mRNA.
EMBL; AY054237; AAL06896.1; -; mRNA.
EMBL; AY058182; AAL25596.1; -; mRNA.
EMBL; AY090382; AAL91284.1; -; mRNA.
EMBL; AF083677; AAN60236.1; -; mRNA.
EMBL; AJ831440; CAH40799.1; -; Genomic_DNA.
EMBL; AJ831441; CAH40800.1; -; Genomic_DNA.
EMBL; AJ831442; CAH40801.1; -; Genomic_DNA.
EMBL; AJ831443; CAH40802.1; -; Genomic_DNA.
EMBL; AJ831444; CAH40803.1; -; Genomic_DNA.
EMBL; AJ831445; CAH40804.1; -; Genomic_DNA.
EMBL; AJ831446; CAH40805.1; -; Genomic_DNA.
EMBL; AJ831447; CAH40806.1; -; Genomic_DNA.
EMBL; AJ831448; CAH40807.1; -; Genomic_DNA.
EMBL; AJ831449; CAH40808.1; -; Genomic_DNA.
EMBL; AJ831450; CAH40809.1; -; Genomic_DNA.
EMBL; AJ831451; CAH40810.1; -; Genomic_DNA.
EMBL; AJ831452; CAH40811.1; -; Genomic_DNA.
EMBL; AJ831453; CAH40812.1; -; Genomic_DNA.
EMBL; AJ831454; CAH40813.1; -; Genomic_DNA.
EMBL; AJ831455; CAH40814.1; -; Genomic_DNA.
EMBL; AJ831456; CAH40815.1; -; Genomic_DNA.
EMBL; AJ831457; CAH40816.1; -; Genomic_DNA.
EMBL; AJ831458; CAH40817.1; -; Genomic_DNA.
EMBL; AJ831459; CAH40818.1; -; Genomic_DNA.
EMBL; AJ831460; CAH40819.1; -; Genomic_DNA.
EMBL; AJ831461; CAH40820.1; -; Genomic_DNA.
EMBL; AJ831462; CAH40821.1; -; Genomic_DNA.
EMBL; AJ831463; CAH40822.1; -; Genomic_DNA.
EMBL; AJ831464; CAH40823.1; -; Genomic_DNA.
EMBL; AJ831465; CAH40824.1; -; Genomic_DNA.
EMBL; AJ831466; CAH40825.1; -; Genomic_DNA.
EMBL; AJ831467; CAH40826.1; -; Genomic_DNA.
EMBL; AK317589; BAH20253.1; -; mRNA.
EMBL; Z18232; CAA79143.1; -; mRNA.
PIR; S56653; S56653.
RefSeq; NP_197972.2; NM_122501.3. [P37702-2]
RefSeq; NP_851077.1; NM_180746.3. [P37702-1]
UniGene; At.23592; -.
UniGene; At.47944; -.
UniGene; At.73176; -.
ProteinModelPortal; P37702; -.
SMR; P37702; -.
BioGrid; 17944; 6.
IntAct; P37702; 1.
STRING; 3702.AT5G26000.1; -.
CAZy; GH1; Glycoside Hydrolase Family 1.
iPTMnet; P37702; -.
SWISS-2DPAGE; P37702; -.
PaxDb; P37702; -.
PRIDE; P37702; -.
EnsemblPlants; AT5G26000.1; AT5G26000.1; AT5G26000. [P37702-1]
EnsemblPlants; AT5G26000.2; AT5G26000.2; AT5G26000. [P37702-2]
GeneID; 832669; -.
Gramene; AT5G26000.1; AT5G26000.1; AT5G26000.
Gramene; AT5G26000.2; AT5G26000.2; AT5G26000.
KEGG; ath:AT5G26000; -.
Araport; AT5G26000; -.
TAIR; locus:2180597; AT5G26000.
eggNOG; KOG0626; Eukaryota.
eggNOG; COG2723; LUCA.
InParanoid; P37702; -.
KO; K01237; -.
OMA; DETKNSY; -.
OrthoDB; EOG093606O7; -.
PhylomeDB; P37702; -.
BioCyc; MetaCyc:AT5G26000-MONOMER; -.
BRENDA; 3.2.1.147; 399.
Reactome; R-ATH-189085; Digestion of dietary carbohydrate.
SABIO-RK; P37702; -.
PRO; PR:P37702; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; P37702; baseline and differential.
Genevisible; P37702; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0008422; F:beta-glucosidase activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0019137; F:thioglucosidase activity; IDA:TAIR.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0002213; P:defense response to insect; IMP:UniProtKB.
GO; GO:0019762; P:glucosinolate catabolic process; IMP:TAIR.
GO; GO:0010119; P:regulation of stomatal movement; IMP:UniProtKB.
GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
GO; GO:0009625; P:response to insect; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
InterPro; IPR001360; Glyco_hydro_1.
InterPro; IPR018120; Glyco_hydro_1_AS.
InterPro; IPR033132; Glyco_hydro_1_N_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR10353; PTHR10353; 1.
Pfam; PF00232; Glyco_hydro_1; 1.
PRINTS; PR00131; GLHYDRLASE1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
1: Evidence at protein level;
Abscisic acid signaling pathway; Alternative splicing;
Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
Hydrolase; Metal-binding; Plant defense; Reference proteome; Signal;
Vacuole; Zinc.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 541 Myrosinase 1.
/FTId=PRO_0000011773.
REGION 475 476 Substrate binding. {ECO:0000250}.
ACT_SITE 420 420 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10055}.
METAL 74 74 Zinc; shared with dimeric partner.
{ECO:0000250}.
METAL 88 88 Zinc; shared with dimeric partner.
{ECO:0000250}.
BINDING 57 57 Substrate. {ECO:0000250}.
BINDING 159 159 Substrate. {ECO:0000250}.
BINDING 204 204 Substrate. {ECO:0000250}.
BINDING 205 205 Ascorbate. {ECO:0000250}.
BINDING 278 278 Ascorbate. {ECO:0000250}.
BINDING 348 348 Substrate. {ECO:0000250}.
BINDING 468 468 Substrate. {ECO:0000250}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 493 493 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 512 512 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 24 449 {ECO:0000250}.
DISULFID 32 445 {ECO:0000250}.
DISULFID 224 232 {ECO:0000250}.
VAR_SEQ 457 541 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_038446.
VARIANT 128 128 S -> N (in strain: cv. Ta-0).
{ECO:0000269|PubMed:15643972}.
VARIANT 261 261 T -> K (in strain: cv. Ba-1).
{ECO:0000269|PubMed:15643972}.
VARIANT 264 264 K -> Q (in strain: cv. Ba-1).
{ECO:0000269|PubMed:15643972}.
VARIANT 427 427 G -> A (in strain: cv. Ag-0, cv. Ba-1,
cv. Mh-0, cv. Mr-0 and Tac-0).
{ECO:0000269|PubMed:15643972}.
VARIANT 459 459 N -> G (in strain: cv. Su-0).
{ECO:0000269|PubMed:15643972}.
VARIANT 489 489 V -> I (in strain: cv. No-0, cv. Rsch-0
and cv. Ta-0).
{ECO:0000269|PubMed:15643972}.
CONFLICT 385 385 P -> H (in Ref. 5; AAL06896).
{ECO:0000305}.
CONFLICT 426 426 P -> A (in Ref. 5; AAL25596).
{ECO:0000305}.
CONFLICT 434 434 A -> T (in Ref. 8; BAH20253).
{ECO:0000305}.
CONFLICT 441 441 I -> N (in Ref. 8; BAH20253).
{ECO:0000305}.
SEQUENCE 541 AA; 61133 MW; 3736B735DE7A5BD1 CRC64;
MKLLMLAFVF LLALATCKGD EFVCEENEPF TCNQTKLFNS GNFEKGFIFG VASSAYQVEG
GRGRGLNVWD SFTHRFPEKG GADLGNGDTT CDSYTLWQKD IDVMDELNST GYRFSIAWSR
LLPKGKRSRG VNPGAIKYYN GLIDGLVAKN MTPFVTLFHW DLPQTLQDEY NGFLNKTIVD
DFKDYADLCF ELFGDRVKNW ITINQLYTVP TRGYALGTDA PGRCSPKIDV RCPGGNSSTE
PYIVAHNQLL AHAAAVDVYR TKYKDDQKGM IGPVMITRWF LPFDHSQESK DATERAKIFF
HGWFMGPLTE GKYPDIMREY VGDRLPEFSE TEAALVKGSY DFLGLNYYVT QYAQNNQTIV
PSDVHTALMD SRTTLTSKNA TGHAPGPPFN AASYYYPKGI YYVMDYFKTT YGDPLIYVTE
NGFSTPGDED FEKATADYKR IDYLCSHLCF LSKVIKEKNV NVKGYFAWSL GDNYEFCNGF
TVRFGLSYVD FANITGDRDL KASGKWFQKF INVTDEDSTN QDLLRSSVSS KNRDRKSLAD
A


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Catalog number Product name Quantity
AS09 449 Antibody: GLUC | beta-glucosidase, Immunogen: native beta- glucosidase purified from almonds, Host: rabbit, polyclonal, Confirmed reactivity: Prunus dulcis 10 mg
AS09 450 Antibody: GLUC | beta-glucosidase, Biotin conjugated, Immunogen: native beta- glucosidase purified from almonds, Host: rabbit, polyclonal, Confirmed reactivity: Prunus dulcis 1 ml
AS09 451 Antibody: GLUC | beta-glucosidase, Affinity purified, Immunogen: native beta- glucosidase purified from almonds, Host: rabbit, polyclonal, Confirmed reactivity: Prunus dulcis 1 mg
9025-38-1 Thioglucosidase from white mustard see 1g
EIAAB25109 Gcs1,Glucosidase 1,Glycoprotein-processing glucosidase I,Mannosyl-oligosaccharide glucosidase,Mogs,Mouse,Mus musculus
M0569 Resorufin beta-D-glucopyranoside, beta-Glucosidase Substrate, 10mg
M0881 Fluorescein di-beta-D-glucopyranoside (FDGlu), beta-Glucosidase Substrate, 5mg
M0065 Fluorescein mono-beta-D-glucopyranoside, Highly fluorescent beta-glucosidase probe, 10mg
AP01229PU-N Glucosidase II beta 100 µg
A4147 beta-Glucosidase, >1000U per MG 100KU
A4147 beta-Glucosidase, >1000U per MG 500KU
orb40824 beta glucosidase antibody 100 ul
abx008826 Beta-glucosidase 2 Antibody 200 μl
GTX101889 Glucosidase 2 subunit beta 100 µl
Z5030050 Beta-Glucosidase Assay Kit 100 assays
orb41845 beta glucosidase antibody 100 ul
orb73378 beta glucosidase antibody 100 ul
orb58815 Rat 1,3-beta D glucosidase ELISA kit 96 wells
orb73377 beta glucosidase antibody 100 ul
AP01229PU-N Glucosidase 2 subunit beta 100 µg
KA1611 beta-Glucosidase Assay Kit 1 Kit
DBGD-100 QuantiChrom™ β-Glucosidase Assay Kit, Quantitative determination of β-glucosidase activity by colorimetric (405nm) method 100Tests
EIAAB25110 Gcs1,Glycoprotein-processing glucosidase I,Mannosyl-oligosaccharide glucosidase,Mogs,Rat,Rattus norvegicus
EIAAB25108 GCS1,Homo sapiens,Human,Mannosyl-oligosaccharide glucosidase,MOGS,Processing A-glucosidase I
DAGD-100 QuantiChrom™ α-Glucosidase Assay Kit, Quantitative determination of α-glucosidase activity by colorimetric (405nm) method 100Tests


 

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