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Indole-3-acetaldehyde oxidase (IAA oxidase) (EC 1.2.3.7) (Aldehyde oxidase 1) (AO-1) (AtAO-1) (AtAO1)

 ALDO1_ARATH             Reviewed;        1368 AA.
Q7G193; O49155; O64417;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
13-FEB-2019, entry version 131.
RecName: Full=Indole-3-acetaldehyde oxidase;
Short=IAA oxidase;
EC=1.2.3.7;
AltName: Full=Aldehyde oxidase 1;
Short=AO-1;
Short=AtAO-1;
Short=AtAO1;
Name=AAO1; Synonyms=AO1; OrderedLocusNames=At5g20960;
ORFNames=F22D1.130;
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], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia; TISSUE=Root;
PubMed=9655945; DOI=10.1016/S0167-4781(98)00085-2;
Hoff T., Frandsen G.I., Rocher A., Mundy J.;
"Biochemical and genetic characterization of three molybdenum cofactor
hydroxylases in Arabidopsis thaliana.";
Biochim. Biophys. Acta 1398:397-402(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
PubMed=9615466; DOI=10.1093/oxfordjournals.pcp.a029387;
Sekimoto H., Seo M., Kawakami N., Komano T., Desloire S.,
Liotenberg S., Marion-Poll A., Caboche M., Kamiya Y., Koshiba T.;
"Molecular cloning and characterization of aldehyde oxidases in
Arabidopsis thaliana.";
Plant Cell Physiol. 39:433-442(1998).
[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;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY, AND CATALYTIC
ACTIVITY.
STRAIN=cv. Columbia;
PubMed=9489015; DOI=10.1104/pp.116.2.687;
Seo M., Akaba S., Oritani T., Delarue M., Bellini C., Caboche M.,
Koshiba T.;
"Higher activity of an aldehyde oxidase in the auxin-overproducing
superroot1 mutant of Arabidopsis thaliana.";
Plant Physiol. 116:687-693(1998).
[6]
SUBUNIT, CATALYTIC ACTIVITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10423535; DOI=10.1093/oxfordjournals.jbchem.a022463;
Akaba S., Seo M., Dohmae N., Takio K., Sekimoto H., Kamiya Y.,
Furuya N., Komano T., Koshiba T.;
"Production of homo- and hetero-dimeric isozymes from two aldehyde
oxidase genes of Arabidopsis thaliana.";
J. Biochem. 126:395-401(1999).
[7]
BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND CATALYTIC
ACTIVITY.
PubMed=10739959; DOI=10.1093/oxfordjournals.jbchem.a022654;
Koiwai H., Akaba S., Seo M., Komano T., Koshiba T.;
"Functional expression of two Arabidopsis aldehyde oxidases in the
yeast Pichia pastoris.";
J. Biochem. 127:659-664(2000).
[8]
TISSUE SPECIFICITY.
PubMed=10972874; DOI=10.1046/j.1365-313x.2000.00812.x;
Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y.,
Koshiba T.;
"Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana.";
Plant J. 23:481-488(2000).
[9]
TISSUE SPECIFICITY.
PubMed=15574845; DOI=10.1093/pcp/pch198;
Seo M., Aoki H., Koiwai H., Kamiya Y., Nambara E., Koshiba T.;
"Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene
family revealed a major role of AAO3 in ABA biosynthesis in seeds.";
Plant Cell Physiol. 45:1694-1703(2004).
-!- FUNCTION: In higher plants aldehyde oxidases (AO) appear to be
homo- and heterodimeric assemblies of AO subunits with probably
different physiological functions. AO-alpha may be involved in the
biosynthesis of auxin, and in biosynthesis of abscisic acid (ABA)
in seeds. In vitro, AO-alpha uses heptaldehyde,
protocatechualdehyde, benzaldehyde, indole-3-aldehyde (IAld),
indole-3-acetaldehyde (IAAld), cinnamaldehyde and citral as
substrates; AO-beta uses IAAld, IAld and naphtaldehyde as
substrates. {ECO:0000269|PubMed:9489015}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + indole-3-acetaldehyde + O2 = (indol-3-yl)acetate +
H(+) + H2O2; Xref=Rhea:RHEA:16277, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
ChEBI:CHEBI:18086, ChEBI:CHEBI:30854; EC=1.2.3.7;
Evidence={ECO:0000269|PubMed:10423535,
ECO:0000269|PubMed:10739959, ECO:0000269|PubMed:9489015};
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250};
Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
Evidence={ECO:0000250};
Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
{ECO:0000250};
-!- ACTIVITY REGULATION: Strongly inhibited by iodoacetate and
potassium cyanide (KCN). Weakly inhibited by 2-mercaptoethanol,
dithiothreitol (DTT), menadione, estradiol, 4'-(9-
acridinylamino)methanesulfon-m-anisidine (mAMSA), allopurinol and
tritonX-100. Not affected by p-chloromercuribenzoate.
{ECO:0000269|PubMed:10739959}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14 uM for heptaldehyde {ECO:0000269|PubMed:10739959};
KM=19 uM for protocatechualdehyde {ECO:0000269|PubMed:10739959};
KM=0.74 uM for benzaldehyde {ECO:0000269|PubMed:10739959};
KM=4.4 uM for indole-3-aldehyde {ECO:0000269|PubMed:10739959};
KM=39 uM for indole-3-acetaldehyde
{ECO:0000269|PubMed:10739959};
KM=20 uM for cinnamaldehyde {ECO:0000269|PubMed:10739959};
KM=22 uM for citral {ECO:0000269|PubMed:10739959};
Vmax=7.1 nmol/min/mg enzyme with heptaldehyde as substrate
{ECO:0000269|PubMed:10739959};
Vmax=8.0 nmol/min/mg enzyme with protocatechualdehyde as
substrate {ECO:0000269|PubMed:10739959};
Vmax=17 nmol/min/mg enzyme with benzaldehyde as substrate
{ECO:0000269|PubMed:10739959};
Vmax=6.9 nmol/min/mg enzyme with IAld as substrate
{ECO:0000269|PubMed:10739959};
Vmax=7.3 nmol/min/mg enzyme with IAAld as substrate
{ECO:0000269|PubMed:10739959};
Vmax=3.8 nmol/min/mg enzyme with cinnamaldehyde as substrate
{ECO:0000269|PubMed:10739959};
Vmax=38 nmol/min/mg enzyme with citral as substrate
{ECO:0000269|PubMed:10739959};
Note=Kinetic values were obtained with the AO-alpha dimer.;
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:10739959};
Temperature dependence:
Optimum temperature is 65 degrees Celsius.
{ECO:0000269|PubMed:10739959};
-!- SUBUNIT: Aldehyde oxidases (AO) are homodimers and heterodimers of
AO subunits. AO-alpha is an AAO1 homodimer; AO-beta is an AAO1-
AAO2 heterodimer. {ECO:0000269|PubMed:10423535}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- TISSUE SPECIFICITY: Predominantly expressed in roots, seedlings,
mature siliques and seeds, and to lower extent in stems and
rosettes. In seedlings, mostly expressed in lower part of
hypocotyls and roots. {ECO:0000269|PubMed:10972874,
ECO:0000269|PubMed:15574845, ECO:0000269|PubMed:9489015,
ECO:0000269|PubMed:9615466, ECO:0000269|PubMed:9655945}.
-!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF039895; AAC39509.1; -; mRNA.
EMBL; AB005804; BAA28624.1; -; mRNA.
EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002688; AED92912.1; -; Genomic_DNA.
EMBL; CP002688; AED92913.1; -; Genomic_DNA.
PIR; T51622; T51622.
PIR; T52049; T52049.
RefSeq; NP_568407.2; NM_122105.3.
RefSeq; NP_851049.1; NM_180718.2.
UniGene; At.19954; -.
ProteinModelPortal; Q7G193; -.
SMR; Q7G193; -.
BioGrid; 17496; 1.
IntAct; Q7G193; 1.
STRING; 3702.AT5G20960.1; -.
PaxDb; Q7G193; -.
PRIDE; Q7G193; -.
EnsemblPlants; AT5G20960.1; AT5G20960.1; AT5G20960.
EnsemblPlants; AT5G20960.2; AT5G20960.2; AT5G20960.
GeneID; 832221; -.
Gramene; AT5G20960.1; AT5G20960.1; AT5G20960.
Gramene; AT5G20960.2; AT5G20960.2; AT5G20960.
KEGG; ath:AT5G20960; -.
Araport; AT5G20960; -.
TAIR; locus:2147127; AT5G20960.
eggNOG; KOG0430; Eukaryota.
eggNOG; COG4630; LUCA.
eggNOG; COG4631; LUCA.
HOGENOM; HOG000191197; -.
InParanoid; Q7G193; -.
KO; K11817; -.
OMA; AKATWVE; -.
OrthoDB; 48717at2759; -.
PhylomeDB; Q7G193; -.
BioCyc; ARA:AT5G20960-MONOMER; -.
BioCyc; MetaCyc:AT5G20960-MONOMER; -.
BRENDA; 1.2.3.1; 399.
Reactome; R-ATH-964975; Vitamins B6 activation to pyridoxal phosphate.
SABIO-RK; Q7G193; -.
PRO; PR:Q7G193; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q7G193; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0004031; F:aldehyde oxidase activity; IDA:TAIR.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IDA:TAIR.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009851; P:auxin biosynthetic process; IMP:TAIR.
InterPro; IPR002888; 2Fe-2S-bd.
InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006058; 2Fe2S_fd_BS.
InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
InterPro; IPR016208; Ald_Oxase/xanthine_DH.
InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
InterPro; IPR005107; CO_DH_flav_C.
InterPro; IPR036683; CO_DH_flav_C_dom_sf.
InterPro; IPR016166; FAD-bd_PCMH.
InterPro; IPR036318; FAD-bd_PCMH-like_sf.
InterPro; IPR002346; Mopterin_DH_FAD-bd.
Pfam; PF01315; Ald_Xan_dh_C; 1.
Pfam; PF02738; Ald_Xan_dh_C2; 1.
Pfam; PF03450; CO_deh_flav_C; 1.
Pfam; PF00941; FAD_binding_5; 1.
Pfam; PF00111; Fer2; 1.
Pfam; PF01799; Fer2_2; 1.
PIRSF; PIRSF000127; Xanthine_DH; 1.
SMART; SM01008; Ald_Xan_dh_C; 1.
SMART; SM01092; CO_deh_flav_C; 1.
SUPFAM; SSF47741; SSF47741; 1.
SUPFAM; SSF54292; SSF54292; 1.
SUPFAM; SSF54665; SSF54665; 1.
SUPFAM; SSF55447; SSF55447; 1.
SUPFAM; SSF56003; SSF56003; 1.
SUPFAM; SSF56176; SSF56176; 1.
PROSITE; PS00197; 2FE2S_FER_1; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51387; FAD_PCMH; 1.
1: Evidence at protein level;
2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis;
Complete proteome; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur;
Metal-binding; Molybdenum; NAD; Oxidoreductase; Reference proteome.
CHAIN 1 1368 Indole-3-acetaldehyde oxidase.
/FTId=PRO_0000166109.
DOMAIN 19 108 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 246 427 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
METAL 60 60 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 65 65 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 68 68 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
CONFLICT 16 16 S -> G (in Ref. 1; AAC39509).
{ECO:0000305}.
CONFLICT 150 150 K -> R (in Ref. 1; AAC39509).
{ECO:0000305}.
CONFLICT 336 343 NVSVLAKI -> MFLCWRKY (in Ref. 1;
AAC39509). {ECO:0000305}.
CONFLICT 624 624 E -> K (in Ref. 1; AAC39509).
{ECO:0000305}.
CONFLICT 708 708 I -> V (in Ref. 1; AAC39509).
{ECO:0000305}.
CONFLICT 1260 1260 W -> L (in Ref. 1; AAC39509).
{ECO:0000305}.
SEQUENCE 1368 AA; 149554 MW; 58C165F4114DC70C CRC64;
MGEKAIDEDK VEAMKSSKTS LVFAINGQRF ELELSSIDPS TTLVDFLRNK TPFKSVKLGC
GEGGCGACVV LLSKYDPLLE KVDEFTISSC LTLLCSIDGC SITTSDGLGN SRVGFHAVHE
RIAGFHATQC GFCTPGMSVS MFSALLNADK SHPPPRSGFS NLTAVEAEKA VSGNLCRCTG
YRPLVDACKS FAADVDIEDL GFNAFCKKGE NRDEVLRRLP CYDHTSSHVC TFPEFLKKEI
KNDMSLHSRK YRWSSPVSVS ELQGLLEVEN GLSVKLVAGN TSTGYYKEEK ERKYERFIDI
RKIPEFTMVR SDEKGVELGA CVTISKAIEV LREEKNVSVL AKIATHMEKI ANRFVRNTGT
IGGNIMMAQR KQFPSDLATI LVAAQATVKI MTSSSSQEQF TLEEFLQQPP LDAKSLLLSL
EIPSWHSAKK NGSSEDSILL FETYRAAPRP LGNALAFLNA AFSAEVTEAL DGIVVNDCQL
VFGAYGTKHA HRAKKVEEFL TGKVISDEVL MEAISLLKDE IVPDKGTSNP GYRSSLAVTF
LFEFFGSLTK KNAKTTNGWL NGGCKEIGFD QNVESLKPEA MLSSAQQIVE NQEHSPVGKG
ITKAGACLQA SGEAVYVDDI PAPENCLYGA FIYSTMPLAR IKGIRFKQNR VPEGVLGIIT
YKDIPKGGQN IGTNGFFTSD LLFAEEVTHC AGQIIAFLVA DSQKHADIAA NLVVIDYDTK
DLKPPILSLE EAVENFSLFE VPPPLRGYPV GDITKGMDEA EHKILGSKIS FGSQYFFYME
TQTALAVPDE DNCMVVYSST QTPEFVHQTI AGCLGVPENN VRVITRRVGG GFGGKAVKSM
PVAAACALAA SKMQRPVRTY VNRKTDMITT GGRHPMKVTY SVGFKSNGKI TALDVEVLLD
AGLTEDISPL MPKGIQGALM KYDWGALSFN VKVCKTNTVS RTALRAPGDV QGSYIGEAII
EKVASYLSVD VDEIRKVNLH TYESLRLFHS AKAGEFSEYT LPLLWDRIDE FSGFNKRRKV
VEEFNASNKW RKRGISRVPA VYAVNMRSTP GRVSVLGDGS IVVEVQGIEI GQGLWTKVKQ
MAAYSLGLIQ CGTTSDELLK KIRVIQSDTL SMVQGSMTAG STTSEASSEA VRICCDGLVE
RLLPVKTALV EQTGGPVTWD SLISQAYQQS INMSVSSKYM PDSTGEYLNY GIAASEVEVN
VLTGETTILR TDIIYDCGKS LNPAVDLGQI EGAFVQGLGF FMLEEFLMNS DGLVVTDSTW
TYKIPTVDTI PRQFNVEILN SGQHKNRVLS SKASGEPPLL LAASVHCAVR AAVKEARKQI
LSWNSNKQGT DMYFELPVPA TMPIVKEFCG LDVVEKYLEW KIQQRKNV


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E0656h ELISA kit ABP,ABP1,Amiloride-binding protein,Amiloride-sensitive amine oxidase [copper-containing],AOC1,DAO,DAO1,Diamine oxidase,Histaminase,Homo sapiens,Human,KAO,Kidney amine oxidase 96T
EIAAB12033 Dual oxidase 2,Duox2,Large NOX 2,Lnox2,Long NOX 2,NADH_NADPH thyroid oxidase THOX2,Rat,Rattus norvegicus,Thox2,Thyroid oxidase 2
EIAAB10105 COX7A2,COX7AL,Cytochrome c oxidase subunit 7A2, mitochondrial,Cytochrome c oxidase subunit VIIaL,Cytochrome c oxidase subunit VIIa-L,Cytochrome c oxidase subunit VIIa-liver_heart,Homo sapiens,Human
EIAAB08786 Canis familiaris,Canis lupus familiaris,COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase sub
EIAAB10086 COX VIa-M,COX6A,COX6A2,COX6AH,COXVIAH,Cytochrome c oxidase polypeptide VIa-heart,Cytochrome c oxidase subunit 6A2, mitochondrial,Cytochrome c oxidase subunit VIA-muscle,Homo sapiens,Human

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP626: Abscisic Acid Biosynthesis
WP617: Ureide biosynthesis
WP1634: Butanoate metabolism
WP1695: Pyruvate metabolism
WP1567: Glycolysis and Gluconeogenesis
WP1581: Histidine metabolism
WP1612: 1,2-Dichloroethane degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1615: 3-Chloroacrylic acid degradation
WP1621: Arginine and proline metabolism
WP1622: Ascorbate and aldarate metabolism
WP1628: beta-Alanine metabolism
WP1655: Geraniol degradation
WP1657: Glycerolipid metabolism
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation
WP1690: Propanoate metabolism
WP1712: Tryptophan metabolism
WP1717: Valine, leucine and isoleucine degradation

Related Genes :
[Aox1 Ao Ro] Aldehyde oxidase 1 (EC 1.2.3.1) (Azaheterocycle hydroxylase 1) (EC 1.17.3.-) (Retinal oxidase)
[Aox3 Aoh1] Aldehyde oxidase 3 (EC 1.2.3.1) (Aldehyde oxidase homolog 1) (Azaheterocycle hydroxylase 3) (EC 1.17.3.-)
[AOX1 AO] Aldehyde oxidase (EC 1.2.3.1) (Aldehyde oxidase 1) (Azaheterocycle hydroxylase) (EC 1.17.3.-)
[AOX1 AO] Aldehyde oxidase 1 (EC 1.2.3.1) (Azaheterocycle hydroxylase 1) (EC 1.17.3.-) (Retinal oxidase) (Retinoic acid synthase)
[AOX1 AO] Aldehyde oxidase 1 (EC 1.2.3.1) (Azaheterocycle hydroxylase 1) (EC 1.17.3.-)
[Aox3 Aoh1] Aldehyde oxidase 3 (EC 1.2.3.1) (Aldehyde oxidase homolog 1) (Azaheterocycle hydroxylase 3) (EC 1.17.3.-)
[Aox1 Ao] Aldehyde oxidase 1 (EC 1.2.3.1) (Azaheterocycle hydroxylase 1) (EC 1.17.3.-)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[AOX1 AO] Aldehyde oxidase 1 (EC 1.2.3.1) (Azaheterocycle hydroxylase 1) (EC 1.17.3.-)
[Aldh3a1 Ahd-4 Ahd4 Aldh3 Aldh4] Aldehyde dehydrogenase, dimeric NADP-preferring (EC 1.2.1.5) (Aldehyde dehydrogenase 4) (Aldehyde dehydrogenase family 3 member A1) (Dioxin-inducible aldehyde dehydrogenase 3)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[ADH2] Aldehyde-alcohol dehydrogenase 2 [Includes: Alcohol dehydrogenase (ADH) (EC 1.1.1.1); Acetaldehyde dehydrogenase (ACDH) (EC 1.2.1.10)]
[wbpB wlbA PA3158] UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate oxidase (EC 1.1.1.335) (UDP-2-acetamido-2-deoxy-alpha-D-glucuronic acid 3-dehydrogenase) (UDP-N-acetyl-D-glucosaminuronic acid 3-oxidase) (UDP-D-GlcNAcA 3-oxidase)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)
[PDC6 YGR087C] Pyruvate decarboxylase isozyme 3 (EC 4.1.1.-) (EC 4.1.1.43) (EC 4.1.1.72) (EC 4.1.1.74) (Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase) (2ODC)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[DUOX2 LNOX2 THOX2] Dual oxidase 2 (EC 1.11.1.-) (EC 1.6.3.1) (Large NOX 2) (Long NOX 2) (NADH/NADPH thyroid oxidase p138-tox) (NADPH oxidase/peroxidase DUOX2) (NADPH thyroid oxidase 2) (Thyroid oxidase 2) (p138 thyroid oxidase)
[AOC1 ABP1] Amiloride-sensitive amine oxidase [copper-containing] (DAO) (Diamine oxidase) (EC 1.4.3.22) (Amiloride-binding protein 1) (Amine oxidase copper domain-containing protein 1) (Histaminase)
[dprE1 MSMEG_6382 MSMEI_6214 LJ00_31545] Decaprenylphosphoryl-beta-D-ribose oxidase (EC 1.1.98.3) (Decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase) (Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE1) (Decaprenyl-phosphoribose 2'-epimerase subunit 1) (Decaprenylphosphoryl-beta-D-ribofuranose 2'-oxidase) (Decaprenylphosphoryl-beta-D-ribose 2-epimerase flavoprotein subunit) (FAD-dependent decaprenylphosphoryl-beta-D-ribofuranose 2-oxidase)
[cydB cyd-2 b0734 JW0723] Cytochrome bd-I ubiquinol oxidase subunit 2 (EC 7.1.1.7) (Cytochrome bd-I oxidase subunit II) (Cytochrome d ubiquinol oxidase subunit II)
[cydA cyd-1 b0733 JW0722] Cytochrome bd-I ubiquinol oxidase subunit 1 (EC 7.1.1.7) (Cytochrome bd-I oxidase subunit I) (Cytochrome d ubiquinol oxidase subunit I)
[cox-1 coi cox1 NCM025 NCU16016] Cytochrome c oxidase subunit 1 (EC 1.9.3.1) (Cytochrome c oxidase polypeptide I)
[COX2 OXI1 Q0250] Cytochrome c oxidase subunit 2 (EC 1.9.3.1) (Cytochrome c oxidase polypeptide II)
[PDC5 YLR134W L3133 L9606.7] Pyruvate decarboxylase isozyme 2 (EC 4.1.1.-) (EC 4.1.1.43) (EC 4.1.1.72) (EC 4.1.1.74) (Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase) (2ODC)
[AOX1A AOX1 HSR3 At3g22370 MCB17.11] Ubiquinol oxidase 1a, mitochondrial (EC 1.10.3.11) (Alternative oxidase 1a)

Bibliography :
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