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LL-diaminopimelate aminotransferase, chloroplastic (AtDAP-AT) (DAP-AT) (DAP-aminotransferase) (LL-DAP-aminotransferase) (EC 2.6.1.83) (Protein ABERRANT GROWTH AND DEATH 2)

 DAPAT_ARATH             Reviewed;         461 AA.
Q93ZN9; O81885;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 110.
RecName: Full=LL-diaminopimelate aminotransferase, chloroplastic;
Short=AtDAP-AT;
Short=DAP-AT;
Short=DAP-aminotransferase;
Short=LL-DAP-aminotransferase;
EC=2.6.1.83 {ECO:0000269|PubMed:16361515, ECO:0000269|PubMed:17583737};
AltName: Full=Protein ABERRANT GROWTH AND DEATH 2;
Flags: Precursor;
Name=DAP; Synonyms=AGD2; OrderedLocusNames=At4g33680;
ORFNames=T16L1.170;
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], MUTAGENESIS OF PRO-398, SUBCELLULAR
LOCATION, INDUCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
PubMed=14729919; DOI=10.1105/tpc.019372;
Song J.T., Lu H., Greenberg J.T.;
"Divergent roles in Arabidopsis thaliana development and defense of
two homologous genes, aberrant growth and death2 and AGD2-LIKE DEFENSE
RESPONSE PROTEIN1, encoding novel aminotransferases.";
Plant Cell 16:353-366(2004).
[2]
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).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=16361515; DOI=10.1104/pp.105.072629;
Hudson A.O., Singh B.K., Leustek T., Gilvarg C.;
"An LL-diaminopimelate aminotransferase defines a novel variant of the
lysine biosynthesis pathway in plants.";
Plant Physiol. 140:292-301(2006).
[6]
FUNCTION.
PubMed=21435399; DOI=10.1016/j.bbapap.2011.03.008;
Watanabe N., James M.N.;
"Structural insights for the substrate recognition mechanism of LL-
diaminopimelate aminotransferase.";
Biochim. Biophys. Acta 1814:1528-1533(2011).
[7]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 36-461 IN COMPLEX WITH
SUBSTRATE ANALOG AND PYRIDOXAL PHOSPHATE, FUNCTION, CATALYTIC
ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
PubMed=17583737; DOI=10.1016/j.jmb.2007.05.061;
Watanabe N., Cherney M.M., van Belkum M.J., Marcus S.L., Flegel M.D.,
Clay M.D., Deyholos M.K., Vederas J.C., James M.N.;
"Crystal structure of LL-diaminopimelate aminotransferase from
Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis
of L-Lysine by plants and Chlamydia.";
J. Mol. Biol. 371:685-702(2007).
[8]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 36-461 OF MUTANTS AND
WILD-TYPE IN COMPLEX WITH SUBSTRATE ANALOG AND PYRIDOXAL PHOSPHATE
ANALOG, FUNCTION, MUTAGENESIS OF LYS-305, COFACTOR, AND SUBUNIT.
PubMed=18952095; DOI=10.1016/j.jmb.2008.10.022;
Watanabe N., Clay M.D., van Belkum M.J., Cherney M.M., Vederas J.C.,
James M.N.;
"Mechanism of substrate recognition and PLP-induced conformational
changes in LL-diaminopimelate aminotransferase from Arabidopsis
thaliana.";
J. Mol. Biol. 384:1314-1329(2008).
-!- FUNCTION: Required for lysine biosynthesis. Catalyzes the direct
conversion of tetrahydrodipicolinate to LL-diaminopimelate, a
reaction that requires three enzymes in E.coli. Not active with
meso-diaminopimelate, lysine or ornithine as substrates.
{ECO:0000269|PubMed:16361515, ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095, ECO:0000269|PubMed:21435399}.
-!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate + 2-oxoglutarate =
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate +
H(2)O. {ECO:0000269|PubMed:16361515, ECO:0000269|PubMed:17583737}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=47 uM for LL-2,6-diaminopimelate
{ECO:0000269|PubMed:17583737};
KM=67 uM for LL-2,6-diaminopimelate
{ECO:0000269|PubMed:16361515};
KM=8.7 mM for 2-oxoglutarate {ECO:0000269|PubMed:16361515};
KM=38 uM for L-2,3,4,5-tetrahydrodipicolinate
{ECO:0000269|PubMed:16361515};
KM=1.9 mM for glutamatic acid {ECO:0000269|PubMed:16361515};
Vmax=22.3 umol/min/mg enzyme for the forward reaction
{ECO:0000269|PubMed:16361515};
Vmax=0.38 umol/min/mg enzyme for the reverse reaction
{ECO:0000269|PubMed:16361515};
pH dependence:
Optimum pH is 7.9 in Tris buffer and 7.6 in HEPES buffer.
{ECO:0000269|PubMed:16361515};
Temperature dependence:
Optimum temperature is 36 degrees Celsius.
{ECO:0000269|PubMed:16361515};
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
(aminotransferase route): step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:14729919}.
-!- TISSUE SPECIFICITY: Highly expressed in seedlings, roots, stems,
flowers and leaves. Lower expression in siliques.
{ECO:0000269|PubMed:14729919}.
-!- DEVELOPMENTAL STAGE: Down-regulated during senescence.
{ECO:0000269|PubMed:14729919}.
-!- INDUCTION: Not induced by pathogen infection, but down-regulated
by dark treatment. {ECO:0000269|PubMed:14729919}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality.
{ECO:0000269|PubMed:14729919}.
-!- MISCELLANEOUS: The expected covalent binding of pyridoxal
phosphate by Lys-305 has not been observed in the 3D-structure.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. LL-diaminopimelate aminotransferase
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA20581.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB80085.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AY518701; AAR99909.1; -; mRNA.
EMBL; AL031394; CAA20581.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161584; CAB80085.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE86265.1; -; Genomic_DNA.
EMBL; AY056423; AAL08279.1; -; mRNA.
EMBL; AY065256; AAL38732.1; -; mRNA.
EMBL; AY117246; AAM51321.1; -; mRNA.
PIR; T04985; T04985.
RefSeq; NP_567934.1; NM_119526.4.
UniGene; At.2456; -.
PDB; 2Z1Z; X-ray; 2.40 A; A/B=36-461.
PDB; 2Z20; X-ray; 1.95 A; A/B=36-461.
PDB; 3EI5; X-ray; 2.05 A; A/B=36-461.
PDB; 3EI6; X-ray; 1.90 A; A/B=36-461.
PDB; 3EI7; X-ray; 1.99 A; A/B=36-461.
PDB; 3EI8; X-ray; 1.60 A; A/B=36-461.
PDB; 3EI9; X-ray; 1.55 A; A/B=36-461.
PDB; 3EIA; X-ray; 1.85 A; A/B=36-461.
PDB; 3EIB; X-ray; 1.85 A; A/B=36-461.
PDBsum; 2Z1Z; -.
PDBsum; 2Z20; -.
PDBsum; 3EI5; -.
PDBsum; 3EI6; -.
PDBsum; 3EI7; -.
PDBsum; 3EI8; -.
PDBsum; 3EI9; -.
PDBsum; 3EIA; -.
PDBsum; 3EIB; -.
ProteinModelPortal; Q93ZN9; -.
SMR; Q93ZN9; -.
BioGrid; 14792; 1.
STRING; 3702.AT4G33680.1; -.
PaxDb; Q93ZN9; -.
PRIDE; Q93ZN9; -.
EnsemblPlants; AT4G33680.1; AT4G33680.1; AT4G33680.
GeneID; 829510; -.
Gramene; AT4G33680.1; AT4G33680.1; AT4G33680.
KEGG; ath:AT4G33680; -.
Araport; AT4G33680; -.
TAIR; locus:2134243; AT4G33680.
eggNOG; KOG0257; Eukaryota.
eggNOG; COG0436; LUCA.
HOGENOM; HOG000223061; -.
InParanoid; Q93ZN9; -.
KO; K10206; -.
OMA; DGSKCDS; -.
OrthoDB; EOG0936094D; -.
PhylomeDB; Q93ZN9; -.
BioCyc; ARA:AT4G33680-MONOMER; -.
BioCyc; MetaCyc:AT4G33680-MONOMER; -.
BRENDA; 2.6.1.83; 399.
SABIO-RK; Q93ZN9; -.
UniPathway; UPA00034; UER00466.
EvolutionaryTrace; Q93ZN9; -.
PRO; PR:Q93ZN9; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q93ZN9; baseline and differential.
Genevisible; Q93ZN9; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IDA:TAIR.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0008483; F:transaminase activity; IDA:TAIR.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:TAIR.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
HAMAP; MF_01642; DapL_aminotrans_1; 1.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR019942; DapL/ALD1.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
PANTHER; PTHR43144; PTHR43144; 1.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR03542; DAPAT_plant; 1.
1: Evidence at protein level;
3D-structure; Aminotransferase; Chloroplast; Complete proteome;
Plastid; Pyridoxal phosphate; Reference proteome; Transferase;
Transit peptide.
TRANSIT 1 36 Chloroplast. {ECO:0000255}.
CHAIN 37 461 LL-diaminopimelate aminotransferase,
chloroplastic.
/FTId=PRO_0000306914.
REGION 163 164 Pyridoxal phosphate binding.
{ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
REGION 302 304 Pyridoxal phosphate binding.
{ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 72 72 Substrate. {ECO:0000269|PubMed:18952095}.
BINDING 99 99 Substrate; via amide nitrogen.
{ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 129 129 Pyridoxal phosphate.
{ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 164 164 Substrate. {ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 187 187 Pyridoxal phosphate.
{ECO:0000269|PubMed:17583737}.
BINDING 187 187 Substrate. {ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 244 244 Pyridoxal phosphate.
{ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 244 244 Substrate. {ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 275 275 Pyridoxal phosphate.
{ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 313 313 Pyridoxal phosphate.
{ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 344 344 Pyridoxal phosphate.
{ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 344 344 Substrate. {ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
BINDING 439 439 Substrate. {ECO:0000269|PubMed:17583737,
ECO:0000269|PubMed:18952095}.
MOD_RES 305 305 N6-(pyridoxal phosphate)lysine.
{ECO:0000269|PubMed:18952095,
ECO:0000305|PubMed:17583737}.
MUTAGEN 305 305 K->N: Loss of LL-DAP-aminotransferase
activity. {ECO:0000269|PubMed:18952095}.
MUTAGEN 305 305 K->Q: Loss of LL-DAP-aminotransferase
activity. {ECO:0000269|PubMed:18952095}.
MUTAGEN 398 398 P->S: In agd2-1; reduced activity and
increased resistance to pathogen.
{ECO:0000269|PubMed:14729919}.
HELIX 63 67 {ECO:0000244|PDB:3EI9}.
HELIX 73 87 {ECO:0000244|PDB:3EI9}.
HELIX 107 119 {ECO:0000244|PDB:3EI9}.
TURN 123 125 {ECO:0000244|PDB:3EI9}.
HELIX 136 147 {ECO:0000244|PDB:3EI9}.
TURN 148 151 {ECO:0000244|PDB:3EI9}.
HELIX 154 156 {ECO:0000244|PDB:3EI9}.
STRAND 157 161 {ECO:0000244|PDB:3EI9}.
HELIX 163 174 {ECO:0000244|PDB:3EI9}.
STRAND 180 185 {ECO:0000244|PDB:3EI9}.
HELIX 189 197 {ECO:0000244|PDB:3EI9}.
TURN 205 208 {ECO:0000244|PDB:3EI9}.
STRAND 214 217 {ECO:0000244|PDB:3EI9}.
HELIX 220 222 {ECO:0000244|PDB:3EI9}.
HELIX 228 230 {ECO:0000244|PDB:3EI9}.
STRAND 235 242 {ECO:0000244|PDB:3EI9}.
TURN 244 246 {ECO:0000244|PDB:3EI9}.
HELIX 252 265 {ECO:0000244|PDB:3EI9}.
STRAND 268 272 {ECO:0000244|PDB:3EI9}.
HELIX 276 278 {ECO:0000244|PDB:3EI9}.
HELIX 287 289 {ECO:0000244|PDB:3EI9}.
HELIX 293 295 {ECO:0000244|PDB:3EI9}.
STRAND 297 303 {ECO:0000244|PDB:3EI9}.
HELIX 304 307 {ECO:0000244|PDB:3EI9}.
TURN 309 312 {ECO:0000244|PDB:3EI9}.
STRAND 315 318 {ECO:0000244|PDB:3EI9}.
HELIX 331 341 {ECO:0000244|PDB:3EI9}.
HELIX 348 357 {ECO:0000244|PDB:3EI9}.
HELIX 360 386 {ECO:0000244|PDB:3EI9}.
STRAND 391 393 {ECO:0000244|PDB:3EI9}.
STRAND 395 403 {ECO:0000244|PDB:3EI9}.
HELIX 409 420 {ECO:0000244|PDB:3EI9}.
HELIX 427 430 {ECO:0000244|PDB:3EI9}.
HELIX 432 434 {ECO:0000244|PDB:3EI9}.
STRAND 437 441 {ECO:0000244|PDB:3EI9}.
HELIX 446 460 {ECO:0000244|PDB:3EI9}.
SEQUENCE 461 AA; 50396 MW; 9F49DE08EEDCEC3D CRC64;
MSSTHQLVSS MISSSSSTFL APSNFNLRTR NACLPMAKRV NTCKCVATPQ EKIEYKTKVS
RNSNMSKLQA GYLFPEIARR RSAHLLKYPD AQVISLGIGD TTEPIPEVIT SAMAKKAHEL
STIEGYSGYG AEQGAKPLRA AIAKTFYGGL GIGDDDVFVS DGAKCDISRL QVMFGSNVTI
AVQDPSYPAY VDSSVIMGQT GQFNTDVQKY GNIEYMRCTP ENGFFPDLST VGRTDIIFFC
SPNNPTGAAA TREQLTQLVE FAKKNGSIIV YDSAYAMYMS DDNPRSIFEI PGAEEVAMET
ASFSKYAGFT GVRLGWTVIP KKLLYSDGFP VAKDFNRIIC TCFNGASNIS QAGALACLTP
EGLEAMHKVI GFYKENTNII IDTFTSLGYD VYGGKNAPYV WVHFPNQSSW DVFAEILEKT
HVVTTPGSGF GPGGEGFVRV SAFGHRENIL EACRRFKQLY K


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EIAAB37900 Endometrial progesterone-induced protein,EPIP,Mouse,Mus musculus,Phosphohydroxythreonine aminotransferase,Phosphoserine aminotransferase,Psa,PSAT,Psat,Psat1
EIAAB39811 AGT,AGT1,AGXT,Alanine--glyoxylate aminotransferase,Homo sapiens,Human,Serine--pyruvate aminotransferase,SPAT,SPT
orb90202 Human Ornithine Aminotransferase protein Ornithine Aminotransferase Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (33-439 a.a.) and ha 5
orb90026 Human Alanine Aminotransferase protein Alanine Aminotransferase Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing having a molecular mass of 54,479 Dalto 1 U
30-187 PSAT1 is likely a phosphoserine aminotransferase, based on similarity to proteins in mouse, rabbit, and Drosophila.The protein encoded by this gene is likely a phosphoserine aminotransferase, based on 0.05 mg
EIAAB28577 Mouse,Mus musculus,Oat,Ornithine aminotransferase, mitochondrial,Ornithine--oxo-acid aminotransferase
EIAAB28575 Bos taurus,Bovine,OAT,Ornithine aminotransferase, mitochondrial,Ornithine--oxo-acid aminotransferase
EIAAB28574 Oat,Ornithine aminotransferase, mitochondrial,Ornithine--oxo-acid aminotransferase,Rat,Rattus norvegicus
LF-PA40003 anti-Aminoadipate Aminotransferase (AADAT) , Rabbit polyclonal to Aminoadipate Aminotransferase (AADAT) , Isotype IgG, Host Rabbit 50 ug
LF-PA40002 anti-Aminoadipate Aminotransferase (AADAT) , Rabbit polyclonal to Aminoadipate Aminotransferase (AADAT) , Isotype IgG, Host Rabbit 50 ug
E5643h Human Ornithine Aminotransferase Like Protein 1 EL 96T
orb90026 Human Alanine Aminotransferase protein Enzymes 1 U
orb90202 Human Ornithine Aminotransferase protein Enzymes 5
183005 Protein,Human Alanine Aminotransferase (r_h_ALT) 100 Units
PE030644h Recombinant human Aspartate aminotransferase, mitochondrial protein 200ug
PE030654h Recombinant human Aspartate aminotransferase, mitochondrial protein 50ug
PE030644h Recombinant human Aspartate aminotransferase, mitochondrial protein 5mg


 

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