Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Aspartate aminotransferase, cytoplasmic (cAspAT) (EC 2.6.1.1) (EC 2.6.1.3) (Cysteine aminotransferase, cytoplasmic) (Cysteine transaminase, cytoplasmic) (cCAT) (Glutamate oxaloacetate transaminase 1) (Transaminase A)

 AATC_CHICK              Reviewed;         412 AA.
P00504;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 140.
RecName: Full=Aspartate aminotransferase, cytoplasmic;
Short=cAspAT;
EC=2.6.1.1;
EC=2.6.1.3;
AltName: Full=Cysteine aminotransferase, cytoplasmic;
AltName: Full=Cysteine transaminase, cytoplasmic;
Short=cCAT;
AltName: Full=Glutamate oxaloacetate transaminase 1;
AltName: Full=Transaminase A;
Name=GOT1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2503046; DOI=10.1016/0300-9084(89)90171-5;
Mattes U., Jaussi R., Ziak M., Juretic N., Lindenmann J.-M.,
Christen P.;
"Structure of cDNA of cytosolic aspartate aminotransferase of chicken
and its expression in E. coli.";
Biochimie 71:411-416(1989).
[2]
PROTEIN SEQUENCE OF 2-412, AND ACETYLATION AT ALA-2.
TISSUE=Heart;
PubMed=499525; DOI=10.1016/0014-5793(79)80537-2;
Shlyapnikov S.V., Myasnikov A.N., Severin E.S., Myagkova M.A.,
Torchinsky Y.M., Braunstein A.E.;
"Primary structure of cytoplasmic aspartate aminotransferase from
chicken heart and its homology with pig heart isoenzymes.";
FEBS Lett. 106:385-388(1979).
[3]
PROTEIN SEQUENCE OF 2-412.
TISSUE=Heart;
Shlyapnikov S.V., Myasnikov A.N., Severin E.S., Myagkova M.A.,
Demidkina T.V., Torchinsky Y.M., Braunstein A.E.;
"Primary structure of cytoplasmic aspartate aminotransferase from
chicken heart IV, Structure of cyanogen bromide peptides and the
complete amino acid sequence of the protein.";
Bioorg. Khim. 6:876-884(1980).
[4]
GENE STRUCTURE.
STRAIN=White leghorn;
PubMed=2401287; DOI=10.1111/j.1432-1033.1990.tb19204.x;
Juretic N., Mattes U., Ziak M., Christen P., Jaussi R.;
"Structure of the genes of two homologous intracellularly heterotopic
isoenzymes. Cytosolic and mitochondrial aspartate aminotransferase of
chicken.";
Eur. J. Biochem. 192:119-126(1990).
[5]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH 2-OXOGLUTARATE.
PubMed=7067826; DOI=10.1016/0014-5793(82)80407-9;
Harutyunyan E.G., Malashkevich V.N., Tersyan S.S., Kochkina V.M.,
Torchinsky Y.M., Braunstein A.E.;
"Three-dimensional structure at 3.2-A resolution of the complex of
cytosolic aspartate aminotransferase from chicken heart with 2-
oxoglutarate.";
FEBS Lett. 138:113-116(1982).
[6]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
PubMed=7360247; DOI=10.1038/284189a0;
Borisov V.V., Borisova S.N., Sosfenov N.I., Vainshtein B.K.;
"Electron density map of chicken heart cytosol aspartate transaminase
at 3.5-A resolution.";
Nature 284:189-190(1980).
[7]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYRODOXAL
PHOSPHATE AND MALEIC ACID, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-258,
AND SUBUNIT.
PubMed=7897655; DOI=10.1006/jmbi.1994.0126;
Malashkevich V.N., Strokopytov B.V., Borisov V.V., Dauter Z.,
Wilson K.S., Torchinsky Y.M.;
"Crystal structure of the closed form of chicken cytosolic aspartate
aminotransferase at 1.9-A resolution.";
J. Mol. Biol. 247:111-124(1995).
-!- FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-
cysteine. Important regulator of levels of glutamate, the major
excitatory neurotransmitter of the vertebrate central nervous
system. Acts as a scavenger of glutamate in brain neuroprotection.
The aspartate aminotransferase activity is involved in hepatic
glucose synthesis during development and in adipocyte
glyceroneogenesis. Using L-cysteine as substrate, regulates levels
of mercaptopyruvate, an important source of hydrogen sulfide.
Mercaptopyruvate is converted into H(2)S via the action of 3-
mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an
important synaptic modulator and neuroprotectant in the brain.
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + L-aspartate = L-glutamate +
oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452,
ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991;
EC=2.6.1.1;
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + L-cysteine = 3-mercaptopyruvate + L-
glutamate; Xref=Rhea:RHEA:17441, ChEBI:CHEBI:16810,
ChEBI:CHEBI:29985, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678;
EC=2.6.1.3;
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:7897655};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7067826,
ECO:0000269|PubMed:7897655}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial
and chloroplastic isozymes.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X15636; CAA33646.1; -; mRNA.
PIR; S05583; XNCHDC.
RefSeq; NP_990652.1; NM_205321.1.
UniGene; Gga.730; -.
PDB; 1AAT; X-ray; 2.80 A; A/B=2-412.
PDB; 2CST; X-ray; 1.90 A; A/B=2-412.
PDBsum; 1AAT; -.
PDBsum; 2CST; -.
ProteinModelPortal; P00504; -.
SMR; P00504; -.
STRING; 9031.ENSGALP00000012086; -.
iPTMnet; P00504; -.
PaxDb; P00504; -.
PRIDE; P00504; -.
GeneID; 396261; -.
KEGG; gga:396261; -.
CTD; 2805; -.
eggNOG; KOG1411; Eukaryota.
eggNOG; COG1448; LUCA.
HOGENOM; HOG000185898; -.
HOVERGEN; HBG000951; -.
InParanoid; P00504; -.
KO; K14454; -.
PhylomeDB; P00504; -.
Reactome; R-GGA-352875; Gluconeogenesis.
Reactome; R-GGA-372568; Amino acid metabolism.
EvolutionaryTrace; P00504; -.
PRO; PR:P00504; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
GO; GO:0047801; F:L-cysteine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
GO; GO:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
GO; GO:0006520; P:cellular amino acid metabolic process; TAS:Reactome.
GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
GO; GO:0006114; P:glycerol biosynthetic process; ISS:UniProtKB.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR000796; Asp_trans.
InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
PANTHER; PTHR11879; PTHR11879; 1.
Pfam; PF00155; Aminotran_1_2; 1.
PRINTS; PR00799; TRANSAMINASE.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Amino-acid biosynthesis; Aminotransferase;
Complete proteome; Cytoplasm; Direct protein sequencing;
Pyridoxal phosphate; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:499525,
ECO:0000269|Ref.3}.
CHAIN 2 412 Aspartate aminotransferase, cytoplasmic.
/FTId=PRO_0000123884.
BINDING 38 38 Aspartate; via amide nitrogen.
BINDING 140 140 Aspartate.
BINDING 194 194 Aspartate.
BINDING 386 386 Aspartate.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:499525}.
MOD_RES 258 258 N6-(pyridoxal phosphate)lysine.
CONFLICT 63 63 D -> N (in Ref. 2; AA sequence and 3; AA
sequence). {ECO:0000305}.
CONFLICT 121 121 Missing (in Ref. 2; AA sequence and 3; AA
sequence). {ECO:0000305}.
CONFLICT 140 140 W -> S (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 175 175 D -> S (in Ref. 2; AA sequence and 3; AA
sequence). {ECO:0000305}.
CONFLICT 232 234 SLD -> NLE (in Ref. 2; AA sequence and 3;
AA sequence). {ECO:0000305}.
TURN 5 8 {ECO:0000244|PDB:2CST}.
HELIX 16 26 {ECO:0000244|PDB:2CST}.
HELIX 51 62 {ECO:0000244|PDB:2CST}.
HELIX 77 88 {ECO:0000244|PDB:2CST}.
HELIX 93 96 {ECO:0000244|PDB:2CST}.
STRAND 100 106 {ECO:0000244|PDB:2CST}.
HELIX 107 122 {ECO:0000244|PDB:2CST}.
STRAND 123 127 {ECO:0000244|PDB:2CST}.
STRAND 133 138 {ECO:0000244|PDB:2CST}.
HELIX 142 149 {ECO:0000244|PDB:2CST}.
STRAND 155 158 {ECO:0000244|PDB:2CST}.
TURN 163 166 {ECO:0000244|PDB:2CST}.
HELIX 170 178 {ECO:0000244|PDB:2CST}.
STRAND 185 192 {ECO:0000244|PDB:2CST}.
TURN 194 196 {ECO:0000244|PDB:2CST}.
HELIX 202 215 {ECO:0000244|PDB:2CST}.
STRAND 218 224 {ECO:0000244|PDB:2CST}.
TURN 226 230 {ECO:0000244|PDB:2CST}.
HELIX 233 236 {ECO:0000244|PDB:2CST}.
HELIX 238 245 {ECO:0000244|PDB:2CST}.
STRAND 250 255 {ECO:0000244|PDB:2CST}.
TURN 257 259 {ECO:0000244|PDB:2CST}.
HELIX 263 265 {ECO:0000244|PDB:2CST}.
STRAND 267 273 {ECO:0000244|PDB:2CST}.
HELIX 277 292 {ECO:0000244|PDB:2CST}.
TURN 293 295 {ECO:0000244|PDB:2CST}.
HELIX 301 311 {ECO:0000244|PDB:2CST}.
HELIX 313 344 {ECO:0000244|PDB:2CST}.
HELIX 352 355 {ECO:0000244|PDB:2CST}.
STRAND 358 362 {ECO:0000244|PDB:2CST}.
HELIX 367 375 {ECO:0000244|PDB:2CST}.
STRAND 386 388 {ECO:0000244|PDB:2CST}.
HELIX 389 391 {ECO:0000244|PDB:2CST}.
TURN 394 396 {ECO:0000244|PDB:2CST}.
HELIX 397 410 {ECO:0000244|PDB:2CST}.
SEQUENCE 412 AA; 45935 MW; C55BEE72669078E1 CRC64;
MAASIFAAVP RAPPVAVFKL TADFREDGDS RKVNLGVGAY RTDEGQPWVL PVVRKVEQLI
AGDGSLNHEY LPILGLPEFR ANASRIALGD DSPAIAQKRV GSVQGLGGTG ALRIGAEFLR
RWYNGNNNTA TPVYVSSPTW ENHNSVFMDA GFKDIRTYRY WDAAKRGLDL QGLLDDMEKA
PEFSIFILHA CAHNPTGTDP TPDEWKQIAA VMKRRCLFPF FDSAYQGFAS GSLDKDAWAV
RYFVSEGFEL FCAQSFSKNF GLYNERVGNL SVVGKDEDNV QRVLSQMEKI VRTTWSNPPS
QGARIVATTL TSPQLFAEWK DNVKTMADRV LLMRSELRSR LESLGTPGTW NHITDQIGMF
SFTGLNPKQV EYMIKEKHIY LMASGRINMC GLTTKNLDYV AKSIHEAVTK IQ


Related products :

Catalog number Product name Quantity
E1214p ELISA Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,GOT1,Pig,Sus scrofa,Transaminase A 96T
U1214p CLIA Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,GOT1,Pig,Sus scrofa,Transaminase A 96T
E1214p ELISA kit Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,GOT1,Pig,Sus scrofa,Transaminase A 96T
E1214m ELISA Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,Got1,Mouse,Mus musculus,Transaminase A 96T
E1214r ELISA Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,Got1,Rat,Rattus norvegicus,Transaminase A 96T
E1214b ELISA Aspartate aminotransferase, cytoplasmic,Bos taurus,Bovine,Glutamate oxaloacetate transaminase 1,GOT1,Transaminase A 96T
E1214r ELISA kit Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,Got1,Rat,Rattus norvegicus,Transaminase A 96T
U1214b CLIA Aspartate aminotransferase, cytoplasmic,Bos taurus,Bovine,Glutamate oxaloacetate transaminase 1,GOT1,Transaminase A 96T
U1214r CLIA Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,Got1,Rat,Rattus norvegicus,Transaminase A 96T
U1214m CLIA Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,Got1,Mouse,Mus musculus,Transaminase A 96T
E1214b ELISA kit Aspartate aminotransferase, cytoplasmic,Bos taurus,Bovine,Glutamate oxaloacetate transaminase 1,GOT1,Transaminase A 96T
E1214m ELISA kit Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,Got1,Mouse,Mus musculus,Transaminase A 96T
E1214Rb ELISA kit Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,GOT1,Oryctolagus cuniculus,Rabbit,Transaminase A 96T
U1214h CLIA Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,GOT1,Homo sapiens,Human,Transaminase A 96T
E1214h ELISA kit Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,GOT1,Homo sapiens,Human,Transaminase A 96T
E1214h ELISA Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,GOT1,Homo sapiens,Human,Transaminase A 96T
E1214Rb ELISA Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,GOT1,Oryctolagus cuniculus,Rabbit,Transaminase A 96T
U1214Rb CLIA Aspartate aminotransferase, cytoplasmic,Glutamate oxaloacetate transaminase 1,GOT1,Oryctolagus cuniculus,Rabbit,Transaminase A 96T
E1214c ELISA kit Aspartate aminotransferase, cytoplasmic,Chicken,Gallus gallus,Glutamate oxaloacetate transaminase 1,GOT1,Transaminase A 96T
E1214c ELISA Aspartate aminotransferase, cytoplasmic,Chicken,Gallus gallus,Glutamate oxaloacetate transaminase 1,GOT1,Transaminase A 96T
U1214c CLIA Aspartate aminotransferase, cytoplasmic,Chicken,Gallus gallus,Glutamate oxaloacetate transaminase 1,GOT1,Transaminase A 96T
18-783-77680 SHEEP ANTI PORCINE GLUTAMIC OXALOACETIC TRANSAMINASE - GOT. Aspartate Transaminase; EC 2.6.1.1; Transaminase A; Glutamate oxaloacetate transaminase 2; mAspAT; Fatty acid-binding protein; FABP-1; FABPp 1 ml
E1612c ELISA kit Aspartate aminotransferase, mitochondrial,Chicken,Gallus gallus,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Transaminase A 96T
E1612c ELISA Aspartate aminotransferase, mitochondrial,Chicken,Gallus gallus,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Transaminase A 96T
U1612c CLIA Aspartate aminotransferase, mitochondrial,Chicken,Gallus gallus,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Transaminase A 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur