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4-chlorobenzoyl coenzyme A dehalogenase (4-CBA-CoA dehalogenase) (4-CBCoA dehalogenase) (4-chlorobenzoyl-CoA dehalogenase) (EC 3.8.1.7)

 CBADH_PSEUC             Reviewed;         269 AA.
A5JTM5;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 1.
12-SEP-2018, entry version 49.
RecName: Full=4-chlorobenzoyl coenzyme A dehalogenase {ECO:0000303|PubMed:7579994};
Short=4-CBA-CoA dehalogenase {ECO:0000312|EMBL:ABQ44578.1};
Short=4-CBCoA dehalogenase {ECO:0000250|UniProtKB:O85078};
Short=4-chlorobenzoyl-CoA dehalogenase {ECO:0000303|PubMed:1610806, ECO:0000303|PubMed:7579994};
EC=3.8.1.7;
Pseudomonas sp. (strain CBS-3).
Bacteria; Proteobacteria.
NCBI_TaxID=72586;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1351742; DOI=10.1021/bi00139a024;
Babbitt P.C., Kenyon G.L., Martin B.M., Charest H., Slyvestre M.,
Scholten J.D., Chang K.H., Liang P.H., Dunaway-Mariano D.;
"Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid
sequence identities among families of acyl:adenyl ligases, enoyl-CoA
hydratases/isomerases, and acyl-CoA thioesterases.";
Biochemistry 31:5594-5604(1992).
[2] {ECO:0000312|EMBL:ABQ44578.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CBS-3;
Zhang W., Dunaway-Mariano D.;
"The nucleotide sequence upstream and downstream of 4-CBA-CoA ORFs in
9.5 kb Pseudomonas sp. strain CBS 3 chromosomal DNA.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305}
PROTEIN SEQUENCE OF 1-40, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
STRAIN=CBS-3;
PubMed=7579994; DOI=10.1007/BF00700458;
Loffler F., Lingens F., Muller R.;
"Dehalogenation of 4-chlorobenzoate. Characterisation of 4-
chlorobenzoyl-coenzyme A dehalogenase from Pseudomonas sp. CBS3.";
Biodegradation 6:203-212(1995).
[4] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, PATHWAY, AND SUBUNIT.
STRAIN=CBS-3;
PubMed=1610806; DOI=10.1021/bi00139a025;
Chang K.H., Liang P.H., Beck W., Scholten J.D., Dunaway-Mariano D.;
"Isolation and characterization of the three polypeptide components of
4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3.";
Biochemistry 31:5605-5610(1992).
[5] {ECO:0000305}
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8218302; DOI=10.1021/bi00096a038;
Liang P.H., Yang G., Dunaway-Mariano D.;
"Specificity of 4-chlorobenzoyl coenzyme A dehalogenase catalyzed
dehalogenation of halogenated aromatics.";
Biochemistry 32:12245-12250(1993).
[6] {ECO:0000305}
ACTIVITY REGULATION, ACTIVE SITES, AND MUTAGENESIS OF GLU-34; GLU-43;
ASP-45; ASP-46; GLU-68; HIS-90; HIS-94; ASP-123; ASP-129; TRP-137;
GLU-163; GLU-175; TRP-179 AND HIS-208.
PubMed=8718880; DOI=10.1021/bi9609533;
Yang G., Liu R.Q., Taylor K.L., Xiang H., Price J.,
Dunaway-Mariano D.;
"Identification of active site residues essential to 4-chlorobenzoyl-
coenzyme A dehalogenase catalysis by chemical modification and site
directed mutagenesis.";
Biochemistry 35:10879-10885(1996).
[7] {ECO:0000305}
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF PHE-64; HIS-81;
PHE-82; TRP-89; HIS-90; GLY-114; TRP-137 AND ASP-145.
PubMed=9063883; DOI=10.1021/bi962765i;
Taylor K.L., Xiang H., Liu R.Q., Yang G., Dunaway-Mariano D.;
"Investigation of substrate activation by 4-chlorobenzoyl-coenzyme A
dehalogenase.";
Biochemistry 36:1349-1361(1997).
[8] {ECO:0000305}
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-24; PHE-64;
ARG-67; GLY-113; GLY-114 AND ARG-257.
PubMed=11747444; DOI=10.1021/bi011536f;
Luo L., Taylor K.L., Xiang H., Wei Y., Zhang W., Dunaway-Mariano D.;
"Role of active site binding interactions in 4-chlorobenzoyl-coenzyme
A dehalogenase catalysis.";
Biochemistry 40:15684-15692(2001).
[9] {ECO:0000305}
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-63; PHE-64;
TYR-65; ALA-112; GLY-113 AND GLY-115.
PubMed=12899635; DOI=10.1021/bi0347656;
Dong J., Lu X., Wei Y., Luo L., Dunaway-Mariano D., Carey P.R.;
"The strength of dehalogenase-substrate hydrogen bonding correlates
with the rate of Meisenheimer intermediate formation.";
Biochemistry 42:9482-9490(2003).
[10] {ECO:0000305}
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-216 AND GLU-232.
PubMed=16388585; DOI=10.1021/bi051477w;
Wu J., Xu D., Lu X., Wang C., Guo H., Dunaway-Mariano D.;
"Contributions of long-range electrostatic interactions to 4-
chlorobenzoyl-CoA dehalogenase catalysis: a combined theoretical and
experimental study.";
Biochemistry 45:102-112(2006).
[11] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT GLN-90 IN COMPLEX
WITH 4-HYDROXYBENZOYL COENZYME A, SUBUNIT, ACTIVE SITE, AND
SUBSTRATE-BINDING SITES.
STRAIN=CBS-3;
PubMed=8679561; DOI=10.1021/bi960768p;
Benning M.M., Taylor K.L., Liu R.-Q., Yang G., Xiang H., Wesenberg G.,
Dunaway-Mariano D., Holden H.M.;
"Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to
1.8 A resolution: an enzyme catalyst generated via adaptive
mutation.";
Biochemistry 35:8103-8109(1996).
[12] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT GLN-90 IN COMPLEX
WITH 4-HYDROXYBENZOYL COENZYME A, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF HIS-90.
PubMed=11695894; DOI=10.1021/bi0114426;
Zhang W., Wei Y., Luo L., Taylor K.L., Yang G., Dunaway-Mariano D.,
Benning M.M., Holden H.M.;
"Histidine 90 function in 4-chlorobenzoyl-coenzyme a dehalogenase
catalysis.";
Biochemistry 40:13474-13482(2001).
-!- FUNCTION: Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA and
4-bromobenzoyl-CoA, but not 4-fluorobenzoyl-CoA. Inactive towards
crotonyl-CoA, alpha-methylcrotonyl-CoA and beta-methylcrotonyl-
CoA. {ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:7579994}.
-!- CATALYTIC ACTIVITY: 4-chlorobenzoyl-CoA + H(2)O = 4-hydroxybenzoyl
CoA + chloride. {ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:7579994}.
-!- ACTIVITY REGULATION: Inactivated by 1 mM Ag(+) and by 5 mM Cu(2+).
Partially inhibited by 5 mM Zn(2+), Mn(2+), Co(2+), Fe(2+) and
Ni(2+). Unaffected by 10 mM Na(+), K(+) and Li(+) and by 0.5 mM
Mg(2+), Mn(2+), Fe(2+), Ca(2+), Co(2+) and Zn(2+). Inhibited by
the sulfhydryl blocking agent 5,5'-dithio-bis-(2-nitrobenzoate),
SDS and N-bromosuccinimide. Unaffected by sodium azide and EDTA.
Inactivated following treatment with diethyl pyrocarbonate; this
inactivation is reversible by treatment with hydroxylamine.
{ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:7579994,
ECO:0000269|PubMed:8718880}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.7 uM for 4-chlorobenzoyl-CoA {ECO:0000269|PubMed:11695894,
ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
ECO:0000269|PubMed:9063883};
KM=4.2 uM for 4-bromobenzoyl-CoA {ECO:0000269|PubMed:11695894,
ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
ECO:0000269|PubMed:9063883};
KM=6.5 uM for 4-iodobenzoyl-CoA {ECO:0000269|PubMed:11695894,
ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
ECO:0000269|PubMed:9063883};
KM=10.4 uM for 2,4-dichlorobenzoyl-CoA
{ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994,
ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883};
KM=42 uM for 3,4-dichlorobenzoyl-CoA
{ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994,
ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883};
KM=30 uM for 4-chloro-2-nitrobenzoyl-CoA
{ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994,
ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883};
KM=5.5 uM for 4-chloro-3-nitrobenzoyl-CoA
{ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994,
ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883};
Vmax=2.2 umol/min/mg enzyme with 4-chlorobenzoyl-CoA as
substrate {ECO:0000269|PubMed:11695894,
ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
ECO:0000269|PubMed:9063883};
pH dependence:
Optimum pH is 10.0. Half maximum activity remains at pH 9.0 and
11.5. Stable from pH 6.5 to 11.0, activity is lost following 10
minutes incubation at pH 4.5 or 12.0.
{ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994,
ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883};
Temperature dependence:
Optimum temperature is 60 degrees Celsius. Retains 60% of
maximum activity at 30 degrees Celsius and 65 degrees Celsius.
After 15 minutes preincubation at 60 degrees Celsius 70% of the
initial activity remains, 15 minutes preincubation at 65 degrees
Celsius results in a total loss of activity.
{ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806,
ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994,
ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883};
-!- PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-
hydroxybenzoate from 4-chlorobenzoate: step 2/3.
{ECO:0000269|PubMed:1610806}.
-!- SUBUNIT: Homotetramer (PubMed:1610806). Homotetramer, homooctamer
and larger multimers (PubMed:7579994). Homotrimer
(PubMed:8679561). {ECO:0000269|PubMed:11695894,
ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:7579994,
ECO:0000269|PubMed:8679561}.
-!- INDUCTION: By 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA or 4-
bromobenzoyl-CoA. {ECO:0000269|PubMed:7579994}.
-!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
{ECO:0000255}.
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EMBL; EF569604; ABQ44578.1; -; Genomic_DNA.
PDB; 1JXZ; X-ray; 1.90 A; A/B/C=1-269.
PDB; 1NZY; X-ray; 1.80 A; A/B/C=1-269.
PDBsum; 1JXZ; -.
PDBsum; 1NZY; -.
ProteinModelPortal; A5JTM5; -.
SMR; A5JTM5; -.
KEGG; ag:ABQ44578; -.
KO; K14418; -.
BioCyc; MetaCyc:MONOMER-14753; -.
BRENDA; 3.8.1.7; 5085.
SABIO-RK; A5JTM5; -.
UniPathway; UPA01011; UER01021.
EvolutionaryTrace; A5JTM5; -.
GO; GO:0018787; F:4-chlorobenzoyl-CoA dehalogenase activity; IDA:UniProtKB.
GO; GO:0015936; P:coenzyme A metabolic process; IDA:UniProtKB.
Gene3D; 1.10.12.10; -; 1.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
InterPro; IPR001753; Enoyl-CoA_hydra/iso.
InterPro; IPR014748; Enoyl-CoA_hydra_C.
Pfam; PF00378; ECH_1; 1.
SUPFAM; SSF52096; SSF52096; 1.
PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Hydrolase.
CHAIN 1 269 4-chlorobenzoyl coenzyme A dehalogenase.
/FTId=PRO_0000401147.
REGION 62 67 Substrate binding.
ACT_SITE 90 90 Proton acceptor.
{ECO:0000269|PubMed:8679561,
ECO:0000269|PubMed:8718880}.
ACT_SITE 145 145 Nucleophile. {ECO:0000269|PubMed:8679561,
ECO:0000269|PubMed:8718880}.
BINDING 24 24 Substrate. {ECO:0000269|PubMed:8679561}.
BINDING 114 114 Substrate; via amide nitrogen.
BINDING 257 257 Substrate; shared with oligomeric
partner.
MUTAGEN 24 24 R->K,L: Does not strongly affect
catalytic activity, but reduces substrate
CoA binding.
{ECO:0000269|PubMed:11747444}.
MUTAGEN 34 34 E->T: Forms inclusion bodies.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 43 43 E->A: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 45 45 D->A: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 46 46 D->A: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 63 63 G->A,I,P: Yields insoluble protein.
{ECO:0000269|PubMed:12899635}.
MUTAGEN 64 64 F->A: 30-fold reduction in catalytic
activity, substrate benzoyl group binding
is unaffected.
{ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635,
ECO:0000269|PubMed:9063883}.
MUTAGEN 64 64 F->L: Retains catalytic activity, but
substrate benzoyl group binding is
decreased. {ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635,
ECO:0000269|PubMed:9063883}.
MUTAGEN 64 64 F->P: Severely reduces catalytic
activity. Arylated intermediate does not
accumulate. {ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635,
ECO:0000269|PubMed:9063883}.
MUTAGEN 65 65 Y->D: Catalytic activity is almost as
efficient as wild type.
{ECO:0000269|PubMed:12899635}.
MUTAGEN 67 67 R->K: Reduces substrate CoA binding.
{ECO:0000269|PubMed:11747444}.
MUTAGEN 67 67 R->L: Forms inclusion bodies.
{ECO:0000269|PubMed:11747444}.
MUTAGEN 68 68 E->T: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 81 81 H->Q: Loss of catalytic activity,
substrate benzoyl group binding is not
affected. {ECO:0000269|PubMed:8718880,
ECO:0000269|PubMed:9063883}.
MUTAGEN 82 82 F->L: Retains catalytic activity, but
substrate benzoyl group binding is
decreased. {ECO:0000269|PubMed:9063883}.
MUTAGEN 89 89 W->F: Retains catalytic activity, but
substrate benzoyl group binding is
decreased. {ECO:0000269|PubMed:9063883}.
MUTAGEN 89 89 W->Y: Reduced activity and substrate
benzoyl group binding.
{ECO:0000269|PubMed:9063883}.
MUTAGEN 90 90 H->Q: Complete loss of catalytic activity
(PubMed:8718880 and PubMed:9063883).
Significantly reduced activity
(PubMed:11695894). Substrate binding is
not significantly affected. Reduced
arylated intermediate formation.
{ECO:0000269|PubMed:11695894,
ECO:0000269|PubMed:8718880,
ECO:0000269|PubMed:9063883}.
MUTAGEN 94 94 H->Q: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 112 112 A->G: Yields insoluble protein.
{ECO:0000269|PubMed:12899635}.
MUTAGEN 112 112 A->S: Protein precipitates upon
purification.
{ECO:0000269|PubMed:12899635}.
MUTAGEN 112 112 A->V: Catalytic activity is almost as
efficient as wild type.
{ECO:0000269|PubMed:12899635}.
MUTAGEN 113 113 G->A: Strongly reduced catalytic activity
and substrate benzoyl group binding.
Arylated intermediate does not
accumulate. {ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635}.
MUTAGEN 113 113 G->N,S: Strongly reduced catalytic
activity. Arylated intermediate does not
accumulate. {ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635}.
MUTAGEN 113 113 G->V: Protein precipitates upon
purification.
{ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:12899635}.
MUTAGEN 114 114 G->A: Strongly reduced catalytic activity
and substrate benzoyl group binding.
{ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:9063883}.
MUTAGEN 114 114 G->P: Unstable.
{ECO:0000269|PubMed:11747444,
ECO:0000269|PubMed:9063883}.
MUTAGEN 115 115 G->L,N,S,V: Yields insoluble protein.
{ECO:0000269|PubMed:12899635}.
MUTAGEN 123 123 D->T: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 129 129 D->T: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 137 137 W->F: Low catalytic activity, but KM
unaffected (PubMed:8718880). Retains
catalytic activity, but substrate benzoyl
group binding is decreased
(PubMed:9063883).
{ECO:0000269|PubMed:8718880,
ECO:0000269|PubMed:9063883}.
MUTAGEN 145 145 D->A: Complete loss of catalytic
activity, but not substrate binding.
{ECO:0000269|PubMed:9063883}.
MUTAGEN 163 163 E->T: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 175 175 E->D: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 179 179 W->F: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 208 208 H->Q: No effect on catalytic activity.
{ECO:0000269|PubMed:8718880}.
MUTAGEN 216 216 R->E,K,L: Yields insoluble protein.
{ECO:0000269|PubMed:16388585}.
MUTAGEN 232 232 E->A,N,Q,R: Yields insoluble protein.
{ECO:0000269|PubMed:16388585}.
MUTAGEN 232 232 E->D: Reduced catalytic activity,
increased substrate binding.
{ECO:0000269|PubMed:16388585}.
MUTAGEN 257 257 R->K: Retains catalytic activity and
substrate CoA binding.
{ECO:0000269|PubMed:11747444}.
MUTAGEN 257 257 R->L: Significantly reduces catalytic
activity and substrate CoA binding.
{ECO:0000269|PubMed:11747444}.
STRAND 3 10 {ECO:0000244|PDB:1NZY}.
STRAND 13 18 {ECO:0000244|PDB:1NZY}.
HELIX 21 23 {ECO:0000244|PDB:1NZY}.
HELIX 29 44 {ECO:0000244|PDB:1NZY}.
STRAND 50 56 {ECO:0000244|PDB:1NZY}.
STRAND 59 61 {ECO:0000244|PDB:1NZY}.
HELIX 66 68 {ECO:0000244|PDB:1NZY}.
STRAND 71 73 {ECO:0000244|PDB:1NZY}.
HELIX 74 98 {ECO:0000244|PDB:1NZY}.
STRAND 99 101 {ECO:0000244|PDB:1NZY}.
STRAND 103 107 {ECO:0000244|PDB:1NZY}.
STRAND 109 112 {ECO:0000244|PDB:1NZY}.
HELIX 114 121 {ECO:0000244|PDB:1NZY}.
STRAND 122 128 {ECO:0000244|PDB:1NZY}.
STRAND 132 134 {ECO:0000244|PDB:1NZY}.
HELIX 137 140 {ECO:0000244|PDB:1NZY}.
HELIX 148 167 {ECO:0000244|PDB:1NZY}.
HELIX 173 178 {ECO:0000244|PDB:1NZY}.
STRAND 183 186 {ECO:0000244|PDB:1NZY}.
HELIX 188 204 {ECO:0000244|PDB:1NZY}.
HELIX 207 220 {ECO:0000244|PDB:1NZY}.
HELIX 225 241 {ECO:0000244|PDB:1NZY}.
HELIX 245 253 {ECO:0000244|PDB:1NZY}.
SEQUENCE 269 AA; 29802 MW; EC165E9063C70B07 CRC64;
MYEAIGHRVE DGVAEITIKL PRHRNALSVK AMQEVTDALN RAEEDDSVGA VMITGAEDAF
CAGFYLREIP LDKGVAGVRD HFRIGALWWH QMIHKIIRVK RPVLAAINGV AAGGGLGISL
ASDMAICADS AKFVCAWHTI GIGNDTATSY SLARIVGMRR AMELMLTNRT LYPEEAKDWG
LVSRVYPKDD FREVAWKVAR ELAAAPTHLQ VMAKERFHAG WMQPVEECTE FEIQNVIASV
THPHFMPCLT EFLDGHRADR PQVELPAGV


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REN-28 Recombinant Human Haloacid Dehalogenase-Like Hydrolase Domain Containing 1 5
CSB-EL011925MO Mouse Iodotyrosine dehalogenase 1(IYD) ELISA kit SpeciesMouse 96T
enz-038 Recombinant Human Haloacid Dehalogenase-Like Hydrolase Domain Containing 2 20
enz-028 Recombinant Human Haloacid Dehalogenase-Like Hydrolase Domain Containing 1 20
E7076h Human Haloacid Dehalogenase Like Hydrolase Domain 96T
enz-038 Recombinant Human Haloacid Dehalogenase-Like Hydrolase Domain Containing 2 5
E13652h Human Haloacid Dehalogenase Like Hydrolase Domain 96T
enz-038 Recombinant Human Haloacid Dehalogenase-Like Hydrolase Domain Containing 2 1mg
CSB-EL011925HU Human Iodotyrosine dehalogenase 1(IYD) ELISA kit SpeciesHuman 96T
enz-028 Recombinant Human Haloacid Dehalogenase-Like Hydrolase Domain Containing 1 1mg
enz-089 Recombinant Human Haloacid Dehalogenase-Like Hydrolase Domain Containing 3 1mg


 

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