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Alpha-aminoadipic semialdehyde synthase (cAt-LKR/SDH) (LKR/SDH) [Includes: Lysine ketoglutarate reductase (LKR) (EC 1.5.1.8); Saccharopine dehydrogenase (EC 1.5.1.9) (cAt-SDH) (SDH)]

 AASS_ARATH              Reviewed;        1064 AA.
Q9SMZ4; O04155; O04156; O04884; Q7DM71; Q947M5; Q94BT4;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-APR-2018, entry version 119.
RecName: Full=Alpha-aminoadipic semialdehyde synthase;
AltName: Full=cAt-LKR/SDH;
Short=LKR/SDH;
Includes:
RecName: Full=Lysine ketoglutarate reductase;
Short=LKR;
EC=1.5.1.8;
Includes:
RecName: Full=Saccharopine dehydrogenase;
EC=1.5.1.9;
AltName: Full=cAt-SDH;
Short=SDH;
Name=LKR/SDH; Synonyms=LKR, SDH; OrderedLocusNames=At4g33150;
ORFNames=F4I10.80;
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] (ISOFORMS LONG AND SHORT), FUNCTION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
PubMed=9286108; DOI=10.1105/tpc.9.8.1305;
Tang G., Miron D., Zhu-Shimoni J.X., Galili G.;
"Regulation of lysine catabolism through lysine-ketoglutarate
reductase and saccharopine dehydrogenase in Arabidopsis.";
Plant Cell 9:1305-1316(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM LONG), AND FUNCTION.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=9426595; DOI=10.1023/A:1005808923191;
Epelbaum S., McDevitt R., Falco S.C.;
"Lysine-ketoglutarate reductase and saccharopine dehydrogenase from
Arabidopsis thaliana: nucleotide sequence and characterization.";
Plant Mol. Biol. 35:735-748(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12226495; DOI=10.1104/pp.005660;
Tang G., Zhu X., Gakiere B., Levanony H., Kahana A., Galili G.;
"The bifunctional LKR/SDH locus of plants also encodes a highly active
monofunctional lysine-ketoglutarate reductase using a polyadenylation
signal located within an intron.";
Plant Physiol. 130:147-154(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 529-1064 (ISOFORM LONG).
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).
[7]
ALTERNATIVE INITIATION.
PubMed=10929113; DOI=10.1046/j.1365-313x.2000.00770.x;
Tang G., Zhu X., Tang X., Galili G.;
"A novel composite locus of Arabidopsis encoding two polypeptides with
metabolically related but distinct functions in lysine catabolism.";
Plant J. 23:195-203(2000).
[8]
SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11080311; DOI=10.1104/pp.124.3.1363;
Zhu X., Tang G., Galili G.;
"Characterization of the two saccharopine dehydrogenase isozymes of
lysine catabolism encoded by the single composite AtLKR/SDH locus of
Arabidopsis.";
Plant Physiol. 124:1363-1371(2000).
[9]
FUNCTION.
PubMed=11500552; DOI=10.1104/pp.126.4.1539;
Zhu X., Tang G., Granier F., Bouchez D., Galili G.;
"A T-DNA insertion knockout of the bifunctional lysine-ketoglutarate
reductase/saccharopine dehydrogenase gene elevates lysine levels in
Arabidopsis seeds.";
Plant Physiol. 126:1539-1545(2001).
[10]
ENZYME REGULATION, SUBUNIT, PHOSPHORYLATION AT THR-238 AND SER-458,
AND MUTAGENESIS OF THR-238; SER-407; SER-458 AND 551-ASN--ARG-554.
PubMed=12393892; DOI=10.1074/jbc.M205466200;
Zhu X., Tang G., Galili G.;
"The activity of the Arabidopsis bifunctional lysine-ketoglutarate
reductase/saccharopine dehydrogenase enzyme of lysine catabolism is
regulated by functional interaction between its two enzyme domains.";
J. Biol. Chem. 277:49655-49661(2002).
[11]
INDUCTION.
PubMed=14576281; DOI=10.1104/pp.103.026294;
Stepansky A., Galili G.;
"Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate
reductase/saccharopine dehydrogenase enzyme of lysine catabolism is
concertedly regulated by metabolic and stress-associated signals.";
Plant Physiol. 133:1407-1415(2003).
[12]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15569707; DOI=10.1093/jxb/eri031;
Stepansky A., Yao Y., Tang G., Galili G.;
"Regulation of lysine catabolism in Arabidopsis through concertedly
regulated synthesis of the two distinct gene products of the composite
AtLKR/SDH locus.";
J. Exp. Bot. 56:525-536(2005).
-!- FUNCTION: Bifunctional enzyme that catalyzes the first two steps
in lysine degradation. The N-terminal and the C-terminal contain
lysine-oxoglutarate reductase and saccharopine dehydrogenase
activity, respectively. Negatively regulates free Lys accumulation
in seeds. {ECO:0000269|PubMed:11500552,
ECO:0000269|PubMed:9286108, ECO:0000269|PubMed:9426595}.
-!- CATALYTIC ACTIVITY: N(6)-(L-1,3-dicarboxypropyl)-L-lysine +
NADP(+) + H(2)O = L-lysine + 2-oxoglutarate + NADPH.
-!- CATALYTIC ACTIVITY: N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+)
+ H(2)O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH.
-!- ENZYME REGULATION: The LKR activity is stimulated by NaCl.
{ECO:0000269|PubMed:12393892}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.180 mM for lysine (isoform Long at pH 7.5 and 30 degrees
Celsius) {ECO:0000269|PubMed:11080311};
KM=0.272 mM for alpha-ketoglutarate (isoform Long at pH 7.5 and
30 degrees Celsius) {ECO:0000269|PubMed:11080311};
KM=0.044 mM for NADPH (isoform Long at pH 7.5 and 30 degrees
Celsius) {ECO:0000269|PubMed:11080311};
KM=0.063 mM for saccharopine (isoform Long at pH 7 and 30
degrees Celsius) {ECO:0000269|PubMed:11080311};
KM=0.035 mM for saccharopine (isoform Long at pH 9 and 30
degrees Celsius) {ECO:0000269|PubMed:11080311};
KM=0.130 mM for saccharopine (isoform Short at pH 7 and 30
degrees Celsius) {ECO:0000269|PubMed:11080311};
KM=0.050 mM for saccharopine (isoform Short at pH 9 and 30
degrees Celsius) {ECO:0000269|PubMed:11080311};
KM=0.374 mM for NAD (isoform Long at pH 7 and 30 degrees
Celsius) {ECO:0000269|PubMed:11080311};
KM=0.698 mM for NAD (isoform Long at pH 9 and 30 degrees
Celsius) {ECO:0000269|PubMed:11080311};
KM=0.333 mM for NAD (isoform Short at pH 7 and 30 degrees
Celsius) {ECO:0000269|PubMed:11080311};
KM=0.759 mM for NAD (isoform Short at pH 9 and 30 degrees
Celsius) {ECO:0000269|PubMed:11080311};
pH dependence:
Optimum pH is 7.5 for LKR activity of isoform Long, and 9 for
SDH activity of both isoforms Long and Short.
{ECO:0000269|PubMed:11080311};
-!- PATHWAY: Amino-acid degradation; L-lysine degradation via
saccharopine pathway; glutaryl-CoA from L-lysine: step 1/6.
-!- PATHWAY: Amino-acid degradation; L-lysine degradation via
saccharopine pathway; glutaryl-CoA from L-lysine: step 2/6.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12393892}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11080311}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Long;
IsoId=Q9SMZ4-1; Sequence=Displayed;
Note=Contains both LKR and SDH activities.;
Name=Short;
IsoId=Q9SMZ4-2; Sequence=VSP_018641;
Note=Contains only SDH activity.;
-!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in flowers.
Isoform Long is mostly present in young leaves, cotyledons, root
tips and mature root parts. Whereas isoform Short is mostly
expressed in cotyledons and at low levels in all root parts.
{ECO:0000269|PubMed:15569707, ECO:0000269|PubMed:9286108}.
-!- DEVELOPMENTAL STAGE: In flowers, confined to ovules and vascular
tissue of anther filament. In developing and mature seeds,
expressed in embryo and the outer layers of the endosperm.
{ECO:0000269|PubMed:9286108}.
-!- INDUCTION: Lysine, Sugar starvation, ABA and MeJA induce isoform
Long, but not isoform Short (at protein level). Nitrogen
starvation repress isoform Long, but not isoform Short (at protein
level). Isoform Long and isoform Short are both slightly induced
by NaCl and drought stress, but repressed by sugars.
{ECO:0000269|PubMed:14576281, ECO:0000269|PubMed:15569707}.
-!- PTM: Phosphorylation of Ser-458 seems important for the LKR
activity. {ECO:0000269|PubMed:12393892}.
-!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT
family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
dehydrogenase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK64010.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAK97099.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Its C-terminal part is derived from gene At1G61240 whose function is unknown. Originally thought to be an alternative splicing form of At4g33150.; Evidence={ECO:0000305};
Sequence=AAM16268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U90522; AAB53975.1; -; mRNA.
EMBL; U90523; AAD00700.1; -; mRNA.
EMBL; U95758; AAB96825.1; -; Genomic_DNA.
EMBL; U95759; AAB96826.1; -; mRNA.
EMBL; AF295389; AAK97099.1; ALT_SEQ; mRNA.
EMBL; AL035525; CAB36789.1; -; Genomic_DNA.
EMBL; AL161583; CAB80032.1; -; Genomic_DNA.
EMBL; CP002687; AEE86184.1; -; Genomic_DNA.
EMBL; AY039906; AAK64010.1; ALT_INIT; mRNA.
EMBL; AY094007; AAM16268.1; ALT_INIT; mRNA.
PIR; T05195; T05195.
RefSeq; NP_001154283.1; NM_001160811.2. [Q9SMZ4-2]
UniGene; At.20921; -.
ProteinModelPortal; Q9SMZ4; -.
SMR; Q9SMZ4; -.
STRING; 3702.AT4G33150.1; -.
iPTMnet; Q9SMZ4; -.
PaxDb; Q9SMZ4; -.
PRIDE; Q9SMZ4; -.
EnsemblPlants; AT4G33150.3; AT4G33150.3; AT4G33150. [Q9SMZ4-2]
GeneID; 829452; -.
Gramene; AT4G33150.3; AT4G33150.3; AT4G33150. [Q9SMZ4-2]
KEGG; ath:AT4G33150; -.
Araport; AT4G33150; -.
eggNOG; KOG0172; Eukaryota.
eggNOG; COG1748; LUCA.
InParanoid; Q9SMZ4; -.
KO; K14157; -.
PhylomeDB; Q9SMZ4; -.
BioCyc; ARA:AT4G33150-MONOMER; -.
Reactome; R-ATH-71064; Lysine catabolism.
SABIO-RK; Q9SMZ4; -.
UniPathway; UPA00868; UER00835.
UniPathway; UPA00868; UER00836.
PRO; PR:Q9SMZ4; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9SMZ4; baseline and differential.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
GO; GO:0004753; F:saccharopine dehydrogenase activity; IBA:GO_Central.
GO; GO:0006091; P:generation of precursor metabolites and energy; IBA:GO_Central.
GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
CDD; cd12144; SDH_N_domain; 1.
InterPro; IPR007886; AlaDH/PNT_N.
InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
InterPro; IPR007545; LOR/SDH_bifunc_enz_cons_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR032095; Sacchrp_dh_C.
InterPro; IPR005097; Sacchrp_dh_NADP.
Pfam; PF05222; AlaDh_PNT_N; 1.
Pfam; PF04455; Saccharop_dh_N; 1.
Pfam; PF16653; Sacchrp_dh_C; 1.
Pfam; PF03435; Sacchrp_dh_NADP; 1.
SMART; SM01002; AlaDh_PNT_C; 1.
SMART; SM01003; AlaDh_PNT_N; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Alternative initiation; Complete proteome; Cytoplasm;
Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphoprotein;
Reference proteome.
CHAIN 1 1064 Alpha-aminoadipic semialdehyde synthase.
/FTId=PRO_0000226070.
NP_BIND 729 731 NADP. {ECO:0000250|UniProtKB:Q9P4R4}.
REGION 24 445 Lysine-ketoglutarate reductase.
REGION 583 1064 Saccharopine dehydrogenase.
REGION 703 704 Saccharopine binding.
{ECO:0000250|UniProtKB:Q9P4R4}.
REGION 852 854 Saccharopine binding.
{ECO:0000250|UniProtKB:Q9P4R4}.
BINDING 730 730 Saccharopine.
{ECO:0000250|UniProtKB:Q9P4R4}.
BINDING 830 830 Saccharopine.
{ECO:0000250|UniProtKB:Q9P4R4}.
MOD_RES 238 238 Phosphothreonine.
{ECO:0000269|PubMed:12393892}.
MOD_RES 458 458 Phosphoserine.
{ECO:0000269|PubMed:12393892}.
VAR_SEQ 1 582 Missing (in isoform Short).
{ECO:0000303|PubMed:9286108}.
/FTId=VSP_018641.
MUTAGEN 238 238 T->A,D: No effect on LKR and SDH
activity. {ECO:0000269|PubMed:12393892}.
MUTAGEN 407 407 S->A: No effect on LKR and SDH activity.
{ECO:0000269|PubMed:12393892}.
MUTAGEN 407 407 S->D: No LKR activity, but no effect on
SDH activity.
{ECO:0000269|PubMed:12393892}.
MUTAGEN 458 458 S->A: Reduced LKR activity, but no effect
on SDH activity.
{ECO:0000269|PubMed:12393892}.
MUTAGEN 458 458 S->D: No effect on LKR and SDH activity.
{ECO:0000269|PubMed:12393892}.
MUTAGEN 551 554 NEDY->IEGR: Loss of LKR activity
stimulation by NaCl.
{ECO:0000269|PubMed:12393892}.
CONFLICT 167 169 KLI -> YLS (in Ref. 1; AAB53975, 2;
AAB96825/AAB96826 and 3; AAK97099).
{ECO:0000305}.
CONFLICT 324 324 R -> S (in Ref. 1; AAB53975 and 3;
AAK97099). {ECO:0000305}.
CONFLICT 621 621 F -> V (in Ref. 6; AAK64010/AAM16268).
{ECO:0000305}.
CONFLICT 715 715 K -> N (in Ref. 1; AAB53975/AAD00700).
{ECO:0000305}.
CONFLICT 735 735 H -> P (in Ref. 1; AAB53975/AAD00700).
{ECO:0000305}.
CONFLICT 739 739 M -> K (in Ref. 1; AAB53975/AAD00700).
{ECO:0000305}.
CONFLICT 746 748 HIK -> PIT (in Ref. 1; AAB53975/
AAD00700). {ECO:0000305}.
CONFLICT 765 765 P -> R (in Ref. 1; AAB53975/AAD00700).
{ECO:0000305}.
CONFLICT 827 827 F -> L (in Ref. 2; AAB96825/AAB96826).
{ECO:0000305}.
CONFLICT 1040 1040 L -> F (in Ref. 2; AAB96825).
{ECO:0000305}.
SEQUENCE 1064 AA; 117149 MW; 6CA4EBDB22898C7E CRC64;
MNSNGHEEEK KLGNGVVGIL AETVNKWERR TPLTPSHCAR LLHGGKDRTG ISRIVVQPSA
KRIHHDALYE DVGCEISDDL SDCGLILGIK QPELEMILPE RAYAFFSHTH KAQKENMPLL
DKILSERVTL CDYELIVGDH GKRLLAFGKY AGRAGLVDFL HGLGQRKLIL GYSTPFLSLG
ASYMYSSLAA AKAAVISVGE EIASQGLPLG ICPLVFVFTG TGNVSLGAQE IFKLLPHTFV
EPSKLPELFV KDKGISQNGI STKRVYQVYG CIITSQDMVE HKDPSKSFDK ADYYAHPEHY
NPVFHEKISP YTSVLVNCMY WEKRFPCLLS TKQLQDLTKK GLPLVGICDI TCDIGGSIEF
VNRATLIDSP FFRFNPSNNS YYDDMDGDGV LCMAVDILPT EFAKEASQHF GDILSGFVGS
LASMTEISDL PAHLKRACIS YRGELTSLYE YIPRMRKSNP EEAQDNIIAN GVSSQRTFNI
LVSLSGHLFD KFLINEALDM IEAAGGSFHL AKCELGQSAD AESYSELEVG ADDKRVLDQI
IDSLTRLANP NEDYISPHRE ANKISLKIGK VQQENEIKEK PEMTKKSGVL ILGAGRVCRP
AADFLASVRT ISSQQWYKTY FGADSEEKTD VHVIVASLYL KDAKETVEGI SDVEAVRLDV
SDSESLLKYV SQVDVVLSLL PASCHAVVAK TCIELKKHLV TASYVDDETS MLHEKAKSAG
ITILGEMGLD PGIDHMMAMK MINDAHIKKG KVKSFTSYCG GLPSPAAANN PLAYKFSWNP
AGAIRAGQNP AKYKSNGDII HVDGKNLYDS AARFRVPNLP AFALECFPNR DSLVYGEHYG
IESEATTIFR GTLRYEGFSM IMATLSKLGF FDSEANQVLS TGKRITFGAL LSNILNKDAD
NESEPLAGEE EISKRIIKLG HSKETAAKAA KTIVFLGFNE EREVPSLCKS VFDATCYLME
EKLAYSGNEQ DMVLLHHEVE VEFLESKRIE KHTATLLEFG DIKNGQTTTA MAKTVGIPAA
IGALLLIEDK IKTRGVLRPL EAEVYLPALD ILQAYGIKLM EKAE


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CSB-EL001028MO Mouse Alpha-aminoadipic semialdehyde synthase, mitochondrial(AASS) ELISA kit 96T
CSB-EL001028BO Bovine Alpha-aminoadipic semialdehyde synthase, mitochondrial(AASS) ELISA kit 96T
CSB-EL001579HU Human Alpha-aminoadipic semialdehyde dehydrogenase(ALDH7A1) ELISA kit 96T
CSB-EL001579RA Rat Alpha-aminoadipic semialdehyde dehydrogenase(ALDH7A1) ELISA kit SpeciesRat 96T
CSB-EL001579BO Bovine Alpha-aminoadipic semialdehyde dehydrogenase(ALDH7A1) ELISA kit 96T
CSB-EL001579MO Mouse Alpha-aminoadipic semialdehyde dehydrogenase(ALDH7A1) ELISA kit 96T
CSB-EL001028MO Mouse Alpha-aminoadipic semialdehyde synthase, mitochondrial(AASS) ELISA kit SpeciesMouse 96T
CSB-EL001028BO Bovine Alpha-aminoadipic semialdehyde synthase, mitochondrial(AASS) ELISA kit SpeciesBovine 96T
CSB-EL001028HU Human Alpha-aminoadipic semialdehyde synthase, mitochondrial(AASS) ELISA kit SpeciesHuman 96T
CSB-EL001579HU Human Alpha-aminoadipic semialdehyde dehydrogenase(ALDH7A1) ELISA kit SpeciesHuman 96T
CSB-EL001579BO Bovine Alpha-aminoadipic semialdehyde dehydrogenase(ALDH7A1) ELISA kit SpeciesBovine 96T
CSB-EL001579MO Mouse Alpha-aminoadipic semialdehyde dehydrogenase(ALDH7A1) ELISA kit SpeciesMouse 96T
AASS_BOVIN ELISA Kit FOR Alpha-aminoadipic semialdehyde synthase, mitochondrial; organism: Bovine; gene name: AASS 96T
AL7A1_BOVIN ELISA Kit FOR Alpha-aminoadipic semialdehyde dehydrogenase; organism: Bovine; gene name: ALDH7A1 96T
EIAAB40021 Aldehyde dehydrogenase family 5 member A1,Aldh5a1,Mouse,Mus musculus,NAD(+)-dependent succinic semialdehyde dehydrogenase,Succinate-semialdehyde dehydrogenase, mitochondrial
EIAAB40019 Aldehyde dehydrogenase family 5 member A1,Aldh5a1,NAD(+)-dependent succinic semialdehyde dehydrogenase,Rat,Rattus norvegicus,Ssadh,Succinate-semialdehyde dehydrogenase, mitochondrial
EIAAB40020 Aldehyde dehydrogenase family 5 member A1,ALDH5A1,Homo sapiens,Human,NAD(+)-dependent succinic semialdehyde dehydrogenase,SSADH,Succinate-semialdehyde dehydrogenase, mitochondrial


 

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