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2,4-dienoyl-CoA reductase (DCR) (EC 1.3.1.34) (2,4-dienoyl-coenzyme A reductase [NADPH])

 FADH_ECOLI              Reviewed;         672 AA.
P42593; Q2M9C5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 161.
RecName: Full=2,4-dienoyl-CoA reductase {ECO:0000303|PubMed:10933894, ECO:0000303|PubMed:9346310};
Short=DCR {ECO:0000303|PubMed:12840019};
EC=1.3.1.34 {ECO:0000269|PubMed:18171025, ECO:0000269|PubMed:6363415, ECO:0000269|PubMed:9346310};
AltName: Full=2,4-dienoyl-coenzyme A reductase [NADPH] {ECO:0000305|PubMed:6363415};
Name=fadH {ECO:0000303|PubMed:9346310}; Synonyms=ygjL;
OrderedLocusNames=b3081, JW3052;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, FUNCTION,
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=K12;
PubMed=9346310; DOI=10.1111/j.1432-1033.1997.00516.x;
He X.-Y., Yang S.-Y., Schulz H.;
"Cloning and expression of the fadH gene and characterization of the
gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli.";
Eur. J. Biochem. 248:516-520(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
ACTIVITY REGULATION, SUBUNIT, INDUCTION, AND PATHWAY.
PubMed=6363415;
Dommes V., Kunau W.H.;
"2,4-Dienoyl coenzyme A reductases from bovine liver and Escherichia
coli. Comparison of properties.";
J. Biol. Chem. 259:1781-1788(1984).
[5]
FUNCTION, COFACTOR, AND PATHWAY.
STRAIN=K12;
PubMed=10933894; DOI=10.1006/abbi.2000.1941;
Liang X., Thorpe C., Schulz H.;
"2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-
sulfur flavoprotein that functions in fatty acid beta-oxidation.";
Arch. Biochem. Biophys. 380:373-379(2000).
[6]
CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS
OF GLU-165; TYR-167; HIS-253 AND CYS-338.
STRAIN=K12;
PubMed=18171025; DOI=10.1021/bi701235t;
Tu X., Hubbard P.A., Kim J.J., Schulz H.;
"Two distinct proton donors at the active site of Escherichia coli
2,4-dienoyl-CoA reductase are responsible for the formation of
different products.";
Biochemistry 47:1167-1175(2008).
[7]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-672 IN COMPLEX WITH
5-MERCAPTOETHANOL-2-DECENOYL-COENZYME A; FAD; FMN; IRON-SULFUR
(4FE-4S) AND NADP, COFACTOR, DOMAIN, REACTION MECHANISM, AND ACTIVE
SITE.
STRAIN=K12;
PubMed=12840019; DOI=10.1074/jbc.M304642200;
Hubbard P.A., Liang X., Schulz H., Kim J.J.;
"The crystal structure and reaction mechanism of Escherichia coli 2,4-
dienoyl-CoA reductase.";
J. Biol. Chem. 278:37553-37560(2003).
-!- FUNCTION: Functions as an auxiliary enzyme in the beta-oxidation
of unsaturated fatty acids with double bonds at even carbon
positions. Catalyzes the NADPH-dependent reduction of the C4-C5
double bond of the acyl chain of 2,4-dienoyl-CoA to yield 2-trans-
enoyl-CoA (PubMed:9346310, PubMed:6363415). Acts on both isomers,
2-trans,4-cis- and 2-trans,4-trans-decadienoyl-CoA, with almost
equal efficiency (PubMed:6363415). Is not active with NADH instead
of NADPH (PubMed:6363415). Does not show cis->trans isomerase
activity (PubMed:10933894). {ECO:0000269|PubMed:10933894,
ECO:0000269|PubMed:6363415, ECO:0000269|PubMed:9346310}.
-!- CATALYTIC ACTIVITY:
Reaction=4,5-saturated-(2E)-enoyl-CoA + NADP(+) = (2E,4E)-dienoyl-
CoA + H(+) + NADPH; Xref=Rhea:RHEA:12136, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85100,
ChEBI:CHEBI:85101; EC=1.3.1.34;
Evidence={ECO:0000269|PubMed:18171025,
ECO:0000269|PubMed:6363415, ECO:0000269|PubMed:9346310};
-!- CATALYTIC ACTIVITY:
Reaction=(2E)-decenoyl-CoA + NADP(+) = (2E,4E)-decadienoyl-CoA +
H(+) + NADPH; Xref=Rhea:RHEA:53296, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61406,
ChEBI:CHEBI:62244; Evidence={ECO:0000269|PubMed:18171025,
ECO:0000269|PubMed:6363415, ECO:0000269|PubMed:9346310};
-!- CATALYTIC ACTIVITY:
Reaction=(2E)-decenoyl-CoA + NADP(+) = (2E,4Z)-decadienoyl-CoA +
H(+) + NADPH; Xref=Rhea:RHEA:53708, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61406,
ChEBI:CHEBI:137593; Evidence={ECO:0000269|PubMed:6363415};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:10933894,
ECO:0000269|PubMed:12840019};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:10933894,
ECO:0000269|PubMed:12840019, ECO:0000269|PubMed:6363415};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000269|PubMed:10933894,
ECO:0000269|PubMed:12840019};
-!- ACTIVITY REGULATION: Is non-competitively inhibited by NADH.
{ECO:0000269|PubMed:6363415}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=50 uM for NADPH {ECO:0000269|PubMed:9346310};
KM=10.1 uM for NADPH {ECO:0000269|PubMed:6363415};
KM=2.3 uM for (2E,4E)-decadienoyl-CoA
{ECO:0000269|PubMed:9346310};
KM=8.8 uM for (2E,4E)-decadienoyl-CoA
{ECO:0000269|PubMed:6363415};
KM=4.1 uM for (2E,4Z)-decadienoyl-CoA
{ECO:0000269|PubMed:6363415};
Note=kcat is 16 sec(-1) for the NADPH-reduction of (2E,4E)-
decadienoyl-CoA. {ECO:0000269|PubMed:9346310};
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
{ECO:0000305|PubMed:10933894, ECO:0000305|PubMed:6363415}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:6363415}.
-!- INTERACTION:
P11349:narH; NbExp=3; IntAct=EBI-561933, EBI-555067;
P19318:narY; NbExp=3; IntAct=EBI-561933, EBI-555059;
-!- INDUCTION: Induced when cells are grown on oleate as sole carbon
source. Repressed by glucose. {ECO:0000269|PubMed:6363415}.
-!- DOMAIN: Is composed of three domains: an N-terminal TIM barrel
(residues 1-368) which binds FMN, the 4Fe-4S cluster, and the
substrate; a flavodoxin-like fold (residues 369-467 and 626-671)
which binds FAD; and an NADP(H)-binding domain (residues 468-625).
{ECO:0000269|PubMed:12840019}.
-!- MISCELLANEOUS: The overall reaction mechanism can be divided into
three stages: initially, reduction of FAD by NADPH, then electron
transfer from FAD to FMN via the 4Fe-4S cluster, and finally
reduction of substrate. {ECO:0000305|PubMed:12840019}.
-!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
oxidoreductase/NADH oxidase family. {ECO:0000305}.
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EMBL; U93405; AAB82738.1; -; Genomic_DNA.
EMBL; U18997; AAA57882.1; -; Genomic_DNA.
EMBL; U00096; AAC76116.1; -; Genomic_DNA.
EMBL; AP009048; BAE77131.1; -; Genomic_DNA.
PIR; F65096; F65096.
RefSeq; NP_417552.1; NC_000913.3.
RefSeq; WP_000121433.1; NZ_LN832404.1.
PDB; 1PS9; X-ray; 2.20 A; A=2-672.
PDBsum; 1PS9; -.
ProteinModelPortal; P42593; -.
SMR; P42593; -.
BioGrid; 4261984; 17.
DIP; DIP-9562N; -.
IntAct; P42593; 10.
STRING; 316385.ECDH10B_3256; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB03698; 5-Mercaptoethanol-2-Decenoyl-Coenzyme A.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB03247; Riboflavin Monophosphate.
SwissLipids; SLP:000001817; -.
PaxDb; P42593; -.
PRIDE; P42593; -.
EnsemblBacteria; AAC76116; AAC76116; b3081.
EnsemblBacteria; BAE77131; BAE77131; BAE77131.
GeneID; 947594; -.
KEGG; ecj:JW3052; -.
KEGG; eco:b3081; -.
PATRIC; fig|511145.12.peg.3176; -.
EchoBASE; EB2582; -.
EcoGene; EG12723; fadH.
eggNOG; ENOG4105CCY; Bacteria.
eggNOG; COG0446; LUCA.
eggNOG; COG1902; LUCA.
HOGENOM; HOG000237760; -.
InParanoid; P42593; -.
KO; K00219; -.
PhylomeDB; P42593; -.
BioCyc; EcoCyc:DIENOYLCOAREDUCT-MONOMER; -.
BioCyc; MetaCyc:DIENOYLCOAREDUCT-MONOMER; -.
BRENDA; 1.3.1.34; 2026.
UniPathway; UPA00659; -.
EvolutionaryTrace; P42593; -.
PRO; PR:P42593; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IDA:EcoCyc.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0033543; P:fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway; IMP:EcoCyc.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR001155; OxRdtase_FMN_N.
Pfam; PF00724; Oxidored_FMN; 1.
Pfam; PF07992; Pyr_redox_2; 1.
SUPFAM; SSF51905; SSF51905; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing;
FAD; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NADP;
Oxidoreductase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9346310}.
CHAIN 2 672 2,4-dienoyl-CoA reductase.
/FTId=PRO_0000194482.
NP_BIND 25 27 FMN. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
NP_BIND 311 312 FMN. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
NP_BIND 563 564 NADP. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
NP_BIND 654 656 NADP. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
NP_BIND 656 658 FAD. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
REGION 253 256 Substrate binding. {ECO:0000244|PDB:1PS9,
ECO:0000305|PubMed:12840019}.
ACT_SITE 167 167 Proton donor.
{ECO:0000305|PubMed:12840019,
ECO:0000305|PubMed:18171025}.
METAL 335 335 Iron-sulfur (4Fe-4S).
{ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
METAL 338 338 Iron-sulfur (4Fe-4S).
{ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
METAL 342 342 Iron-sulfur (4Fe-4S).
{ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
METAL 354 354 Iron-sulfur (4Fe-4S).
{ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 59 59 FMN; via amide nitrogen.
{ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 101 101 FMN. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 176 176 Substrate. {ECO:0000244|PDB:1PS9,
ECO:0000305|PubMed:12840019}.
BINDING 215 215 FMN. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 289 289 FMN; via amide nitrogen.
{ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 340 340 FAD. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 340 340 NADP. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 385 385 FAD; via amide nitrogen.
{ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 404 404 FAD. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 412 412 FAD. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 422 422 FAD. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 449 449 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
BINDING 567 567 Substrate. {ECO:0000244|PDB:1PS9,
ECO:0000305|PubMed:12840019}.
BINDING 578 578 Substrate. {ECO:0000244|PDB:1PS9,
ECO:0000305|PubMed:12840019}.
BINDING 649 649 FAD; via amide nitrogen.
{ECO:0000244|PDB:1PS9,
ECO:0000269|PubMed:12840019}.
SITE 253 253 Important for catalytic activity, assists
active site Tyr in protonation of C4.
{ECO:0000305|PubMed:12840019,
ECO:0000305|PubMed:18171025}.
MUTAGEN 165 165 E->A: Exhibits 1.3% of wild-type
activity. {ECO:0000269|PubMed:18171025}.
MUTAGEN 165 165 E->Q: Loss of enzyme activity; when
associated with Ala-167.
{ECO:0000269|PubMed:18171025}.
MUTAGEN 167 167 Y->F: Forms 3-enoyl-CoA as the product of
the reaction instead of 2-enoyl-CoA, at a
rate which is 26% of wild-type. 2-fold
increase in substrate affinity. Loss of
enzyme activity; when associated with
Gln-165. {ECO:0000269|PubMed:18171025}.
MUTAGEN 253 253 H->A: 1000-fold reduction in enzyme
activity. Forms both 3-enoyl-CoA and 2-
enoyl-CoA as products of the reaction.
{ECO:0000269|PubMed:18171025}.
MUTAGEN 253 253 H->F: Loss of enzyme activity.
{ECO:0000269|PubMed:18171025}.
MUTAGEN 338 338 C->A: 1000-fold reduction in enzyme
activity. Highly affects iron-sulfur
cluster binding.
{ECO:0000269|PubMed:18171025}.
TURN 4 7 {ECO:0000244|PDB:1PS9}.
STRAND 16 23 {ECO:0000244|PDB:1PS9}.
HELIX 36 49 {ECO:0000244|PDB:1PS9}.
STRAND 53 64 {ECO:0000244|PDB:1PS9}.
HELIX 78 80 {ECO:0000244|PDB:1PS9}.
HELIX 81 93 {ECO:0000244|PDB:1PS9}.
STRAND 98 102 {ECO:0000244|PDB:1PS9}.
HELIX 106 108 {ECO:0000244|PDB:1PS9}.
STRAND 109 111 {ECO:0000244|PDB:1PS9}.
STRAND 115 119 {ECO:0000244|PDB:1PS9}.
HELIX 134 153 {ECO:0000244|PDB:1PS9}.
STRAND 157 163 {ECO:0000244|PDB:1PS9}.
HELIX 168 173 {ECO:0000244|PDB:1PS9}.
TURN 175 177 {ECO:0000244|PDB:1PS9}.
STRAND 185 187 {ECO:0000244|PDB:1PS9}.
HELIX 188 206 {ECO:0000244|PDB:1PS9}.
STRAND 208 219 {ECO:0000244|PDB:1PS9}.
HELIX 228 241 {ECO:0000244|PDB:1PS9}.
STRAND 244 250 {ECO:0000244|PDB:1PS9}.
STRAND 259 261 {ECO:0000244|PDB:1PS9}.
TURN 266 269 {ECO:0000244|PDB:1PS9}.
HELIX 270 276 {ECO:0000244|PDB:1PS9}.
STRAND 284 286 {ECO:0000244|PDB:1PS9}.
HELIX 293 301 {ECO:0000244|PDB:1PS9}.
STRAND 306 311 {ECO:0000244|PDB:1PS9}.
HELIX 313 316 {ECO:0000244|PDB:1PS9}.
HELIX 320 325 {ECO:0000244|PDB:1PS9}.
HELIX 329 331 {ECO:0000244|PDB:1PS9}.
TURN 340 342 {ECO:0000244|PDB:1PS9}.
HELIX 343 347 {ECO:0000244|PDB:1PS9}.
TURN 358 361 {ECO:0000244|PDB:1PS9}.
TURN 363 365 {ECO:0000244|PDB:1PS9}.
STRAND 376 380 {ECO:0000244|PDB:1PS9}.
HELIX 384 394 {ECO:0000244|PDB:1PS9}.
TURN 395 397 {ECO:0000244|PDB:1PS9}.
STRAND 399 409 {ECO:0000244|PDB:1PS9}.
HELIX 413 416 {ECO:0000244|PDB:1PS9}.
HELIX 425 439 {ECO:0000244|PDB:1PS9}.
STRAND 442 446 {ECO:0000244|PDB:1PS9}.
STRAND 451 454 {ECO:0000244|PDB:1PS9}.
STRAND 457 462 {ECO:0000244|PDB:1PS9}.
STRAND 466 468 {ECO:0000244|PDB:1PS9}.
TURN 475 477 {ECO:0000244|PDB:1PS9}.
STRAND 481 483 {ECO:0000244|PDB:1PS9}.
HELIX 484 488 {ECO:0000244|PDB:1PS9}.
STRAND 496 501 {ECO:0000244|PDB:1PS9}.
HELIX 504 514 {ECO:0000244|PDB:1PS9}.
HELIX 521 523 {ECO:0000244|PDB:1PS9}.
HELIX 525 531 {ECO:0000244|PDB:1PS9}.
HELIX 541 543 {ECO:0000244|PDB:1PS9}.
STRAND 555 561 {ECO:0000244|PDB:1PS9}.
TURN 568 571 {ECO:0000244|PDB:1PS9}.
TURN 574 576 {ECO:0000244|PDB:1PS9}.
HELIX 577 586 {ECO:0000244|PDB:1PS9}.
STRAND 590 592 {ECO:0000244|PDB:1PS9}.
STRAND 596 601 {ECO:0000244|PDB:1PS9}.
STRAND 604 609 {ECO:0000244|PDB:1PS9}.
STRAND 612 616 {ECO:0000244|PDB:1PS9}.
STRAND 619 623 {ECO:0000244|PDB:1PS9}.
STRAND 627 629 {ECO:0000244|PDB:1PS9}.
HELIX 634 638 {ECO:0000244|PDB:1PS9}.
TURN 639 641 {ECO:0000244|PDB:1PS9}.
STRAND 644 646 {ECO:0000244|PDB:1PS9}.
HELIX 648 650 {ECO:0000244|PDB:1PS9}.
HELIX 658 671 {ECO:0000244|PDB:1PS9}.
SEQUENCE 672 AA; 72678 MW; B26C7CAAACE760C3 CRC64;
MSYPSLFAPL DLGFTTLKNR VLMGSMHTGL EEYPDGAERL AAFYAERARH GVALIVSGGI
APDLTGVGME GGAMLNDASQ IPHHRTITEA VHQEGGKIAL QILHTGRYSY QPHLVAPSAL
QAPINRFVPH ELSHEEILQL IDNFARCAQL AREAGYDGVE VMGSEGYLIN EFLTLRTNQR
SDQWGGDYRN RMRFAVEVVR AVRERVGNDF IIIYRLSMLD LVEDGGTFAE TVELAQAIEA
AGATIINTGI GWHEARIPTI ATPVPRGAFS WVTRKLKGHV SLPLVTTNRI NDPQVADDIL
SRGDADMVSM ARPFLADAEL LSKAQSGRAD EINTCIGCNQ ACLDQIFVGK VTSCLVNPRA
CHETKMPILP AVQKKNLAVV GAGPAGLAFA INAAARGHQV TLFDAHSEIG GQFNIAKQIP
GKEEFYETLR YYRRMIEVTG VTLKLNHTVT ADQLQAFDET ILASGIVPRT PPIDGIDHPK
VLSYLDVLRD KAPVGNKVAI IGCGGIGFDT AMYLSQPGES TSQNIAGFCN EWGIDSSLQQ
AGGLSPQGMQ IPRSPRQIVM LQRKASKPGQ GLGKTTGWIH RTTLLSRGVK MIPGVSYQKI
DDDGLHVVIN GETQVLAVDN VVICAGQEPN RALAQPLIDS GKTVHLIGGC DVAMELDARR
AIAQGTRLAL EI


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enz-102 Recombinant Human 2,4-Dienoyl CoA Reductase 1 10
enz-211 Recombinant Human 2,4-Dienoyl CoA Reductase 2 1mg
enz-102 Recombinant Human 2,4-Dienoyl CoA Reductase 1 1mg
enz-211 Recombinant Human 2,4-Dienoyl CoA Reductase 2 10
enz-102 Recombinant Human 2,4-Dienoyl CoA Reductase 1 2
enz-211 Recombinant Human 2,4-Dienoyl CoA Reductase 2 2
REN-102 Recombinant Human 2,4-Dienoyl CoA Reductase 1 2
REN-211 Recombinant Human 2,4-Dienoyl CoA Reductase 2 2
enz-102 Recombinant Human 24-Dienoyl CoA Reductase 1 ENZYMES 10
enz-102 Recombinant Human 2,4-Dienoyl CoA Reductase 1 DECR1 2
enz-102 Recombinant Human 2,4-Dienoyl CoA Reductase 1 DECR1 10
7-02647 Recombinant Human 2,4-Dienoyl CoA Reductase 1 2
enz-102 Recombinant Human 2,4-Dienoyl CoA Reductase 1 DECR1 1mg
enz-102 Recombinant Human 24-Dienoyl CoA Reductase 1 ENZYMES 1mg
enz-211 Recombinant Human 24-Dienoyl CoA Reductase 2 ENZYMES 1mg
7-02649 Recombinant Human 2,4-Dienoyl CoA Reductase 1 1mg
enz-211 Recombinant Human 24-Dienoyl CoA Reductase 2 ENZYMES 10


 

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