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

Scytalone dehydratase (SD) (SDH) (EC 4.2.1.94)

 SCYD_MAGO7              Reviewed;         172 AA.
P56221; A4QTI6; G4N445;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 1.
20-DEC-2017, entry version 110.
RecName: Full=Scytalone dehydratase {ECO:0000303|PubMed:9571787};
Short=SD {ECO:0000303|PubMed:9539706};
Short=SDH {ECO:0000303|PubMed:9571787};
EC=4.2.1.94 {ECO:0000269|PubMed:10320327, ECO:0000269|PubMed:10386945, ECO:0000269|PubMed:9466791, ECO:0000269|PubMed:9466792, ECO:0000269|PubMed:9539706, ECO:0000269|PubMed:9571787};
Name=SDH1; ORFNames=MGG_05059;
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice
blast fungus) (Pyricularia oryzae).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Magnaporthales; Magnaporthaceae;
Magnaporthe.
NCBI_TaxID=242507;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=9571787; DOI=10.1271/bbb.62.564;
Motoyama T., Imanishi K., Yamaguchi I.;
"cDNA cloning, expression, and mutagenesis of scytalone dehydratase
needed for pathogenicity of the rice blast fungus, Pyricularia
oryzae.";
Biosci. Biotechnol. Biochem. 62:564-566(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
PubMed=15846337; DOI=10.1038/nature03449;
Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W.,
Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J.,
Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E.,
Birren B.W.;
"The genome sequence of the rice blast fungus Magnaporthe grisea.";
Nature 434:980-986(2005).
[3]
PROTEIN SEQUENCE OF 95-106, AND INDUCTION.
PubMed=15378734; DOI=10.1002/pmic.200400969;
Kim S.T., Yu S., Kim S.G., Kim H.J., Kang S.Y., Hwang D.H., Jang Y.S.,
Kang K.Y.;
"Proteome analysis of rice blast fungus (Magnaporthe grisea) proteome
during appressorium formation.";
Proteomics 4:3579-3587(2004).
[4]
CRYSTALLIZATION.
PubMed=8355286; DOI=10.1006/jmbi.1993.1449;
Lundqvist T., Weber P.C., Hodge C.N., Braswell E.H., Rice J.,
Pierce J.;
"Preliminary crystallographic studies on scytalone dehydratase from
Magnaporthe grisea.";
J. Mol. Biol. 232:999-1002(1993).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9466791; DOI=10.1006/abio.1997.2489;
Thompson J.E., Basarab G.S., Pierce J., Hodge C.N., Jordan D.B.;
"2,3-Dihydro-2,5-dihydroxy-4H-benzopyran-4-one: a nonphysiological
substrate for fungal melanin biosynthetic enzymes.";
Anal. Biochem. 256:1-6(1998).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=9466792; DOI=10.1006/abio.1997.2490;
Thompson J.E., Jordan D.B.;
"Partition analysis of an enzyme acting concurrently upon two
substrates in a continuous multiwavelength assay.";
Anal. Biochem. 256:7-13(1998).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
PubMed=9539706; DOI=10.1073/pnas.95.8.4158;
Zheng Y.J., Bruice T.C.;
"Role of a critical water in scytalone dehydratase-catalyzed
reaction.";
Proc. Natl. Acad. Sci. U.S.A. 95:4158-4163(1998).
[8]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE
SITE, AND MUTAGENESIS OF TYR-30; ASP-31; TYR-50; HIS-85; HIS-110;
SER-129 AND ASN-131.
PubMed=10320327; DOI=10.1021/bi982952b;
Basarab G.S., Steffens J.J., Wawrzak Z., Schwartz R.S., Lundqvist T.,
Jordan D.B.;
"Catalytic mechanism of scytalone dehydratase: site-directed
mutagenisis, kinetic isotope effects, and alternate substrates.";
Biochemistry 38:6012-6024(1999).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=10386945; DOI=10.1016/S0960-894X(99)00246-2;
Jordan D.B., Lessen T.A., Wawrzak Z., Bisaha J.J., Gehret T.C.,
Hansen S.L., Schwartz R.S., Basarab G.S.;
"Design of scytalone dehydratase inhibitors as rice blast fungicides:
(N-phenoxypropyl)-carboxamides.";
Bioorg. Med. Chem. Lett. 9:1607-1612(1999).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=10386946; DOI=10.1016/S0960-894X(99)00247-4;
Basarab G.S., Jordan D.B., Gehret T.C., Schwartz R.S., Wawrzak Z.;
"Design of scytalone dehydratase inhibitors as rice blast fungicides:
derivatives of norephedrine.";
Bioorg. Med. Chem. Lett. 9:1613-1618(1999).
[11]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=10694394; DOI=10.1021/bi991839y;
Jordan D.B., Zheng Y.J., Lockett B.A., Basarab G.S.;
"Stereochemistry of the enolization of scytalone by scytalone
dehydratase.";
Biochemistry 39:2276-2282(2000).
[12]
FUNCTION, CATALYTIC ACTIVITY, INHIBITOR-BINDING, AND MUTAGENESIS OF
PHE-53; MET-69; VAL-75; PHE-158 AND PHE-162.
PubMed=10913266; DOI=10.1021/bi000467m;
Jordan D.B., Basarab G.S., Steffens J.J., Schwartz R.S., Doughty J.G.;
"Tight binding inhibitors of scytalone dehydratase: effects of site-
directed mutations.";
Biochemistry 39:8593-8602(2000).
[13]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-30; TYR-50;
HIS-85; HIS-110 AND ASN-131.
PubMed=10636235; DOI=10.1016/S0960-894X(99)00586-7;
Jordan D.B., Basarab G.S.;
"Binding dynamics of two water molecules constrained within the
scytalone dehydratase binding pocket.";
Bioorg. Med. Chem. Lett. 10:23-26(2000).
[14]
ENZYME REGULATION.
PubMed=10882002; DOI=10.1016/S0968-0896(00)00034-1;
Jennings L.D., Rayner D.R., Jordan D.B., Okonya J.F., Basarab G.S.,
Amorose D.K., Anaclerio B.M., Lee J.K., Schwartz R.S., Whitmore K.A.;
"Cyclobutane carboxamide inhibitors of fungal melanin: biosynthesis
and their evaluation as fungicides.";
Bioorg. Med. Chem. 8:897-907(2000).
[15]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF PHE-53; HIS-110 AND ASN-131.
PubMed=11790103; DOI=10.1021/bi015848u;
Zheng Y.J., Basarab G.S., Jordan D.B.;
"Roles of substrate distortion and intramolecular hydrogen bonding in
enzymatic catalysis by scytalone dehydratase.";
Biochemistry 41:820-826(2002).
[16]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=12413868; DOI=10.1016/S0968-0896(02)00272-9;
Basarab G.S., Jordan D.B., Gehret T.C., Schwartz R.S.;
"Design of inhibitors of scytalone dehydratase: probing interactions
with an asparagine carboxamide.";
Bioorg. Med. Chem. 10:4143-4154(2002).
[17]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND MUTAGENESIS OF
VAL-75.
PubMed=15056895; DOI=10.1271/bbb.68.615;
Yamada N., Motoyama T., Nakasako M., Kagabu S., Kudo T., Yamaguchi I.;
"Enzymatic characterization of scytalone dehydratase Val75Met variant
found in melanin biosynthesis dehydratase inhibitor (MBI-D) resistant
strains of the rice blast fungus.";
Biosci. Biotechnol. Biochem. 68:615-621(2004).
[18]
ENZYME REGULATION, AND MUTAGENESIS OF VAL-75.
PubMed=15382507; DOI=10.1002/ps.896;
Takagaki M., Kaku K., Watanabe S., Kawai K., Shimizu T., Sawada H.,
Kumakura K., Nagayama K.;
"Mechanism of resistance to carpropamid in Magnaporthe grisea.";
Pest Manag. Sci. 60:921-926(2004).
[19]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH INHIBITOR,
SUBUNIT, AND ACTIVE SITE.
PubMed=7866745; DOI=10.1016/S0969-2126(94)00095-6;
Lundqvist T., Rice J., Hodge C.N., Basarab G.S., Pierce J.,
Lindqvist Y.;
"Crystal structure of scytalone dehydratase -- a disease determinant
of the rice pathogen, Magnaporthe grisea.";
Structure 2:937-944(1994).
[20]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH INHIBITOR
CARPROPAMID.
PubMed=9665698; DOI=10.1021/bi980321b;
Nakasako M., Motoyama T., Kurahashi Y., Yamaguchi I.;
"Cryogenic X-ray crystal structure analysis for the complex of
scytalone dehydratase of a rice blast fungus and its tight-binding
inhibitor, carpropamid: the structural basis of tight-binding
inhibition.";
Biochemistry 37:9931-9939(1998).
[21]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 10-172 IN COMPLEX WITH
INHIBITOR.
PubMed=9922139; DOI=10.1021/bi981848r;
Chen J.M., Xu S.L., Wawrzak Z., Basarab G.S., Jordan D.B.;
"Structure-based design of potent inhibitors of scytalone dehydratase:
displacement of a water molecule from the active site.";
Biochemistry 37:17735-17744(1998).
[22]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 10-172 IN COMPLEX WITH
INHIBITOR.
PubMed=10382670;
DOI=10.1002/(SICI)1097-0134(19990601)35:4<425::AID-PROT6>3.0.CO;2-1;
Wawrzak Z., Sandalova T., Steffens J.J., Basarab G.S., Lundqvist T.,
Lindqvist Y., Jordan D.B.;
"High-resolution structures of scytalone dehydratase-inhibitor
complexes crystallized at physiological pH.";
Proteins 35:425-439(1999).
[23]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
PubMed=11752795; DOI=10.1107/S0907444901017371;
Motoyama T., Nakasako M., Yamaguchi I.;
"Crystallization of scytalone dehydratase F162A mutant in the
unligated state and a preliminary X-ray diffraction study at 37 K.";
Acta Crystallogr. D 58:148-150(2002).
-!- FUNCTION: Scytalone dehydratase; part of the gene cluster that
mediates the biosynthesis of dihydroxynaphthalene melanin, a
bluish-green pigment and a structural component of the conidial
wall (PubMed:9571787). Within the pathway, catalyzes the
dehydration of scytalone as well as of vermelone (PubMed:9571787,
PubMed:9466791, PubMed:9466792, PubMed:9539706, PubMed:10320327,
PubMed:10386945, PubMed:10386946, PubMed:10694394,
PubMed:10913266, PubMed:10636235, PubMed:11790103,
PubMed:12413868, PubMed:15056895). Is also able to dehydrate the
alternate substrate 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one
(DDBO) to 5-hydroxy-4H-1-benzopyran-4-one (HBO) (PubMed:9466791,
PubMed:9466792, PubMed:10320327, PubMed:10386945,
PubMed:11790103). {ECO:0000269|PubMed:10320327,
ECO:0000269|PubMed:10386945, ECO:0000269|PubMed:10386946,
ECO:0000269|PubMed:10636235, ECO:0000269|PubMed:10694394,
ECO:0000269|PubMed:10913266, ECO:0000269|PubMed:11790103,
ECO:0000269|PubMed:12413868, ECO:0000269|PubMed:15056895,
ECO:0000269|PubMed:9466791, ECO:0000269|PubMed:9466792,
ECO:0000269|PubMed:9539706, ECO:0000269|PubMed:9571787}.
-!- CATALYTIC ACTIVITY: Scytalone = 1,3,8-trihydroxynaphthalene +
H(2)O. {ECO:0000269|PubMed:10320327, ECO:0000269|PubMed:10386945,
ECO:0000269|PubMed:10386946, ECO:0000269|PubMed:10636235,
ECO:0000269|PubMed:10694394, ECO:0000269|PubMed:10913266,
ECO:0000269|PubMed:11790103, ECO:0000269|PubMed:12413868,
ECO:0000269|PubMed:15056895, ECO:0000269|PubMed:9466791,
ECO:0000269|PubMed:9466792, ECO:0000269|PubMed:9539706,
ECO:0000269|PubMed:9571787}.
-!- ENZYME REGULATION: (N-phenoxypropyl)-carboxamides such as
carpropamid and derivatives of norephedrine act as inhibitors of
scytalone dehydratase activity. {ECO:0000269|PubMed:10386945,
ECO:0000269|PubMed:10386946, ECO:0000269|PubMed:10882002,
ECO:0000269|PubMed:12413868, ECO:0000269|PubMed:15056895,
ECO:0000269|PubMed:15382507}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=15 uM for 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one
(DDBO) {ECO:0000269|PubMed:10320327,
ECO:0000269|PubMed:9466791};
KM=33 uM for scytalone {ECO:0000269|PubMed:10320327};
KM=31 uM for vermelone {ECO:0000269|PubMed:10320327,
ECO:0000269|PubMed:11790103};
-!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
{ECO:0000269|PubMed:9571787}.
-!- SUBUNIT: Homotrimer (PubMed:7866745). Each subunit contains an
active site, located in the central part of the hydrophobic core
of the monomer, which functions independently (PubMed:7866745).
{ECO:0000269|PubMed:7866745}.
-!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:O14434}.
-!- INDUCTION: Expression is induced in the stationary phase, when
melanin synthesis occurs (PubMed:9571787). Expression is
specifically induced during appressorium formation
(PubMed:15378734). {ECO:0000269|PubMed:15378734,
ECO:0000269|PubMed:9571787}.
-!- SIMILARITY: Belongs to the scytalone dehydratase family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB004741; BAA34046.1; -; mRNA.
EMBL; CM001233; EHA52765.1; -; Genomic_DNA.
RefSeq; XP_003712572.1; XM_003712524.1.
PDB; 1IDP; X-ray; 1.45 A; A/B/C=1-172.
PDB; 1STD; X-ray; 2.90 A; A=1-172.
PDB; 2STD; X-ray; 2.10 A; A=1-172.
PDB; 3STD; X-ray; 1.65 A; A/B/C=10-172.
PDB; 4STD; X-ray; 2.15 A; A/B/C=10-172.
PDB; 5STD; X-ray; 1.95 A; A/B/C=10-172.
PDB; 6STD; X-ray; 1.80 A; A/B/C=10-172.
PDB; 7STD; X-ray; 1.80 A; A/B/C=10-172.
PDBsum; 1IDP; -.
PDBsum; 1STD; -.
PDBsum; 2STD; -.
PDBsum; 3STD; -.
PDBsum; 4STD; -.
PDBsum; 5STD; -.
PDBsum; 6STD; -.
PDBsum; 7STD; -.
ProteinModelPortal; P56221; -.
SMR; P56221; -.
BindingDB; P56221; -.
ChEMBL; CHEMBL2578; -.
EnsemblFungi; MGG_05059T0; MGG_05059T0; MGG_05059.
GeneID; 2675492; -.
KEGG; mgr:MGG_05059; -.
EuPathDB; FungiDB:MGG_05059; -.
InParanoid; P56221; -.
KO; K17740; -.
OrthoDB; EOG092C4YYV; -.
BRENDA; 4.2.1.94; 3152.
UniPathway; UPA00785; -.
EvolutionaryTrace; P56221; -.
PRO; PR:P56221; -.
Proteomes; UP000009058; Chromosome 3.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030411; F:scytalone dehydratase activity; IEA:UniProtKB-EC.
GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR032710; NTF2-like_dom_sf.
InterPro; IPR004235; Scytalone_dehydratase.
Pfam; PF02982; Scytalone_dh; 1.
PIRSF; PIRSF024851; SCD1; 1.
ProDom; PD022193; Scytalone_dehydratase; 1.
SUPFAM; SSF54427; SSF54427; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Direct protein sequencing;
Endosome; Lyase; Melanin biosynthesis; Metal-binding;
Reference proteome.
CHAIN 1 172 Scytalone dehydratase.
/FTId=PRO_0000097639.
ACT_SITE 85 85 {ECO:0000305|PubMed:7866745}.
ACT_SITE 110 110 {ECO:0000305|PubMed:7866745}.
BINDING 30 30 Substrate. {ECO:0000305|PubMed:9922139}.
BINDING 50 50 Substrate. {ECO:0000305|PubMed:9665698}.
BINDING 53 53 Substrate; via carbonyl oxygen.
{ECO:0000305|PubMed:10382670}.
BINDING 131 131 Substrate. {ECO:0000305|PubMed:10382670,
ECO:0000305|PubMed:7866745,
ECO:0000305|PubMed:9922139}.
MUTAGEN 30 30 Y->F: Results in a 9-fold decrease of
activity with scytalone as the substrate
and increases binding of salicylamide
inhibitors. {ECO:0000269|PubMed:10320327,
ECO:0000269|PubMed:10636235}.
MUTAGEN 31 31 D->N: Reduces catalysis 5000-fold and
substrate affinity about 4-fold with
scytalone as the substrate.
{ECO:0000269|PubMed:10320327}.
MUTAGEN 50 50 Y->F: Results in a 500-fold decrease of
activity with scytalone as the substrate
and increases binding of salicylamide
inhibitors. {ECO:0000269|PubMed:10320327,
ECO:0000269|PubMed:10636235}.
MUTAGEN 53 53 F->A: Leads to significantly higher
relative substrate specificities
(DDBO/vermelone).
{ECO:0000269|PubMed:11790103}.
MUTAGEN 53 53 F->L: Affects the binding of inhibitors
and has significantly higher relative
substrate specificities (DDBO/vermelone).
{ECO:0000269|PubMed:10913266,
ECO:0000269|PubMed:11790103}.
MUTAGEN 69 69 M->L: Affects the binding of inhibitors.
{ECO:0000269|PubMed:10913266}.
MUTAGEN 75 75 V->A: Affects the binding of inhibitors
and reduces more than 200-fold inhibition
by carpropamid.
{ECO:0000269|PubMed:10913266,
ECO:0000269|PubMed:15056895}.
MUTAGEN 75 75 V->M: Reduces strongly inhibition by
carpropamid.
{ECO:0000269|PubMed:15382507}.
MUTAGEN 85 85 H->N: Greatly decreases catalytic
efficiency and decreases binding to
salicylamide inhibitors.
{ECO:0000269|PubMed:10320327,
ECO:0000269|PubMed:10636235}.
MUTAGEN 110 110 H->N: Causes a 250-fold decrease of
activity and a 6-fold increase in Km with
scytalone as the substrate, decreases
binding of salicylamide inhibitors, and
has significantly higher relative
substrate specificities (DDBO/vermelone).
{ECO:0000269|PubMed:10320327,
ECO:0000269|PubMed:10636235,
ECO:0000269|PubMed:11790103}.
MUTAGEN 129 129 S->A: Results in a 80-fold decrease of
activity and a 7-fold increase in Km with
scytalone as the substrate.
{ECO:0000269|PubMed:10320327}.
MUTAGEN 129 129 S->T: Results in a 120-fold decrease of
activity and a 23-fold increase in Km
with scytalone as the substrate.
{ECO:0000269|PubMed:10320327}.
MUTAGEN 131 131 N->A: Decreases turnover by nearly 90-
fold and increases Km 8-fold with
scytalone as the substrate, decreases
strongly binding of salicylamide
inhibitors, and has significantly higher
relative substrate specificities
(DDBO/vermelone).
{ECO:0000269|PubMed:10320327,
ECO:0000269|PubMed:10636235,
ECO:0000269|PubMed:11790103}.
MUTAGEN 158 158 F->L: Affects the binding of inhibitors.
{ECO:0000269|PubMed:10913266}.
MUTAGEN 162 162 F->L: Affects the binding of inhibitors.
{ECO:0000269|PubMed:10913266}.
HELIX 13 32 {ECO:0000244|PDB:1IDP}.
HELIX 35 39 {ECO:0000244|PDB:1IDP}.
STRAND 42 49 {ECO:0000244|PDB:1IDP}.
HELIX 51 54 {ECO:0000244|PDB:1IDP}.
STRAND 57 62 {ECO:0000244|PDB:1IDP}.
HELIX 63 71 {ECO:0000244|PDB:1IDP}.
TURN 73 76 {ECO:0000244|PDB:1IDP}.
STRAND 81 83 {ECO:0000244|PDB:1IDP}.
STRAND 86 96 {ECO:0000244|PDB:1IDP}.
STRAND 99 115 {ECO:0000244|PDB:1IDP}.
STRAND 121 138 {ECO:0000244|PDB:1IDP}.
STRAND 141 155 {ECO:0000244|PDB:1IDP}.
HELIX 158 161 {ECO:0000244|PDB:3STD}.
HELIX 163 169 {ECO:0000244|PDB:3STD}.
SEQUENCE 172 AA; 20250 MW; 2FA56296D5EE00DC CRC64;
MGSQVQKSDE ITFSDYLGLM TCVYEWADSY DSKDWDRLRK VIAPTLRIDY RSFLDKLWEA
MPAEEFVGMV SSKQVLGDPT LRTQHFIGGT RWEKVSEDEV IGYHQLRVPH QRYKDTTMKE
VTMKGHAHSA NLHWYKKIDG VWKFAGLKPD IRWGEFDFDR IFEDGRETFG DK


Related products :

Catalog number Product name Quantity
49598-85-8 Scytalone 3,4-Dihydro-3,6,8-trihyd 1g
EIAAB25736 APAF1-interacting protein,APIP,Bos taurus,Bovine,MTRu-1-P dehydratase,Probable methylthioribulose-1-phosphate dehydratase
EIAAB25735 APAF1-interacting protein,APIP,CGI-29,Homo sapiens,Human,MTRu-1-P dehydratase,Probable methylthioribulose-1-phosphate dehydratase
EIAAB37755 Homo sapiens,Human,L-serine deaminase,L-serine dehydratase_L-threonine deaminase,L-threonine dehydratase,SDH 2,SDSL,Serine dehydratase 2,Serine dehydratase-like,TDH
EIAAB25733 APAF1-interacting protein,Apip,Mmrp19,Monocyte_macrophage protein 19,Mouse,MTRu-1-P dehydratase,Mus musculus,Probable methylthioribulose-1-phosphate dehydratase
EIAAB25734 APAF1-interacting protein homolog,APIP,Chicken,Gallus gallus,MTRu-1-P dehydratase,Probable methylthioribulose-1-phosphate dehydratase,RCJMB04_5f12
EIAAB37754 L-serine deaminase,L-serine dehydratase_L-threonine deaminase,L-threonine dehydratase,Mouse,Mus musculus,SDH,Sds,Sdsl,Serine dehydratase-like,TDH
EIAAB39937 D-serine ammonia-lyase,D-serine dehydratase,Homo sapiens,Human,L-serine ammonia-lyase,L-serine dehydratase,Serine racemase,SRR
EIAAB39936 D-serine ammonia-lyase,D-serine dehydratase,L-serine ammonia-lyase,L-serine dehydratase,Mouse,Mus musculus,Serine racemase,Srr
EIAAB39935 Bos taurus,Bovine,D-serine ammonia-lyase,D-serine dehydratase,L-serine ammonia-lyase,L-serine dehydratase,Serine racemase,SRR
EIAAB39934 D-serine ammonia-lyase,D-serine dehydratase,L-serine ammonia-lyase,L-serine dehydratase,Rat,Rattus norvegicus,Serine racemase,Srr
833 5_AMINOLEVULINATE DEHYDRATASE, BLOOD 1
SDS SDS Gene serine dehydratase
enz-180 Recombinant Human Serine Dehydratase-Like 1mg
REN-586 Recombinant Human Aminolevulinate Dehydratase 2
orb74125 GDP mannose 4,6 dehydratase antibody 100 ul
C246 Pterin-4-a-Carbinolamine Dehydratase PHS 500
C246 Pterin-4-a-Carbinolamine Dehydratase PHS lmg
E13812272 serine Dehydratase (SDS) ELISA Kit 1
REN-191 Recombinant Human GDP-Mannose 4,6-Dehydratase 5
enz-586 Recombinant Human Aminolevulinate Dehydratase 1mg
REN-180 Recombinant Human Serine Dehydratase-Like 2
enz-191 Recombinant Human GDP-Mannose 4,6-Dehydratase 5
enz-586 Recombinant Human Aminolevulinate Dehydratase 2
enz-180 Recombinant Human Serine Dehydratase-Like 2


 

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 Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | 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

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
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 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
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | 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
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

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