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

Angiotensin-converting enzyme (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II)

 ACE_DROME               Reviewed;         615 AA.
Q10714; A4V0P3; Q27572; Q9NKE4; Q9TX66; Q9VJV3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 3.
25-OCT-2017, entry version 163.
RecName: Full=Angiotensin-converting enzyme;
EC=3.4.15.1;
AltName: Full=Dipeptidyl carboxypeptidase I;
AltName: Full=Kininase II;
Flags: Precursor;
Name=Ance; Synonyms=Race; ORFNames=CG8827;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=8224398; DOI=10.1042/bst021243s;
Cornell M.J., Coates D., Isaac R.E.;
"Characterisation of putative Drosophila angiotensin converting enzyme
cDNA clones.";
Biochem. Soc. Trans. 21:243-243(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND ENZYME REGULATION.
PubMed=7775412; DOI=10.1074/jbc.270.23.13613;
Cornell M.J., Williams T.A., Lamango N.S., Coates D., Corvol P.,
Soubrier F., Hoheisel J., Lehrach H., Isaac R.E.;
"Cloning and expression of an evolutionary conserved single-domain
angiotensin converting enzyme from Drosophila melanogaster.";
J. Biol. Chem. 270:13613-13619(1995).
[3]
SEQUENCE REVISION.
Cornell M.J.;
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Canton-S;
PubMed=7547464; DOI=10.1016/0925-4773(95)00349-5;
Tatei K., Cai H., Ip Y.T., Levine M.;
"Race: a Drosophila homologue of the angiotensin converting enzyme.";
Mech. Dev. 51:157-168(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10471707;
Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G.,
Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G.,
Martin C., Moshrefi A.R., Palazzolo M., Reese M.G., Spradling A.C.,
Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.;
"An exploration of the sequence of a 2.9-Mb region of the genome of
Drosophila melanogaster: the Adh region.";
Genetics 153:179-219(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[7]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[9]
CLEAVAGE SITE, GLYCOSYLATION, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8761461; DOI=10.1042/bj3180125;
Williams T.A., Michaud A., Houard X., Chauvet M.-T., Soubrier F.,
Corvol P.;
"Drosophila melanogaster angiotensin I-converting enzyme expressed in
Pichia pastoris resembles the C domain of the mammalian homologue and
does not require glycosylation for secretion and enzymic activity.";
Biochem. J. 318:125-131(1996).
[10]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9839949; DOI=10.1046/j.1432-1327.1998.2570599.x;
Houard X., Williams T.A., Michaud A., Dani P., Isaac R.E.,
Shirras A.D., Coates D., Corvol P.;
"The Drosophila melanogaster-related angiotensin-I-converting enzymes
Acer and Ance -- distinct enzymic characteristics and alternative
expression during pupal development.";
Eur. J. Biochem. 257:599-606(1998).
[11]
TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12591244; DOI=10.1016/S0012-1606(02)00082-9;
Hurst D., Rylett C.M., Isaac R.E., Shirras A.D.;
"The Drosophila angiotensin-converting enzyme homologue Ance is
required for spermiogenesis.";
Dev. Biol. 254:238-247(2003).
[12]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 14-615, X-RAY CRYSTALLOGRAPHY
(2.4 ANGSTROMS) OF 14-615 IN COMPLEX WITH CAPTOPRIL, AND X-RAY
CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-615 IN COMPLEX WITH LISINOPRIL.
PubMed=12633854; DOI=10.1016/S0014-5793(03)00128-5;
Kim H.M., Shin D.R., Yoo O.J., Lee H., Lee J.-O.;
"Crystal structure of Drosophila angiotensin I-converting enzyme bound
to captopril and lisinopril.";
FEBS Lett. 538:65-70(2003).
-!- FUNCTION: May be involved in the specific maturation or
degradation of a number of bioactive peptides. May play a role in
the contractions of the heart, gut and testes, and in spermatid
differentiation. {ECO:0000269|PubMed:12591244}.
-!- CATALYTIC ACTIVITY: Release of a C-terminal dipeptide,
oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither
Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II,
with increase in vasoconstrictor activity, but no action on
angiotensin II. {ECO:0000269|PubMed:7775412}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- ENZYME REGULATION: Inhibited by captopril and, to a lesser extent,
by lisinopril, trandolaprilat, fosinoprilat and enalaprilat.
{ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=33.5 uM for angiotensin I {ECO:0000269|PubMed:7775412,
ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949};
KM=53.4 uM for N-acetyl-Ser-Asp-Lys-Pro
{ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461,
ECO:0000269|PubMed:9839949};
KM=2.59 mM for Hip-His-Leu {ECO:0000269|PubMed:7775412,
ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949};
KM=10.26 mM for Hip-His-Leu-NH(2) {ECO:0000269|PubMed:7775412,
ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949};
KM=372 uM for (Leu5)enkephalin {ECO:0000269|PubMed:7775412,
ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949};
KM=1.88 mM for (Leu5)enkephalinamide
{ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461,
ECO:0000269|PubMed:9839949};
-!- INTERACTION:
P01019:AGT (xeno); NbExp=2; IntAct=EBI-115736, EBI-751728;
P01042:KNG1 (xeno); NbExp=2; IntAct=EBI-115736, EBI-6378713;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- TISSUE SPECIFICITY: Expressed in vesicular structures in
spermatocytes and early spermatids (at protein level).
{ECO:0000269|PubMed:12591244}.
-!- DEVELOPMENTAL STAGE: Expressed in the amnioserosa during germ band
elongation, shortening and heart morphogenesis. Expressed in
midgut throughout embryogenesis.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:8761461}.
-!- DISRUPTION PHENOTYPE: Male flies are sterile.
{ECO:0000269|PubMed:12591244}.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U25344; AAB02171.1; -; mRNA.
EMBL; U34599; AAC46902.1; -; mRNA.
EMBL; AE014134; AAF53353.2; -; Genomic_DNA.
EMBL; AE014134; AAN10856.1; -; Genomic_DNA.
EMBL; AY061129; AAL28677.1; -; mRNA.
RefSeq; NP_001285915.1; NM_001298986.1.
RefSeq; NP_477046.1; NM_057698.5.
RefSeq; NP_723852.1; NM_165070.3.
UniGene; Dm.2157; -.
PDB; 1J36; X-ray; 2.40 A; A/B=14-615.
PDB; 1J37; X-ray; 2.40 A; A/B=14-615.
PDB; 1J38; X-ray; 2.60 A; A/B=14-615.
PDB; 2X8Y; X-ray; 1.90 A; A=17-614.
PDB; 2X8Z; X-ray; 1.98 A; A=17-614.
PDB; 2X90; X-ray; 1.98 A; A=17-614.
PDB; 2X91; X-ray; 1.98 A; A=17-614.
PDB; 2X92; X-ray; 2.11 A; A=17-615.
PDB; 2X93; X-ray; 1.98 A; A=17-615.
PDB; 2X94; X-ray; 1.88 A; A=17-615.
PDB; 2X95; X-ray; 1.96 A; A=17-615.
PDB; 2X96; X-ray; 1.85 A; A=17-614.
PDB; 2X97; X-ray; 1.85 A; A=17-614.
PDB; 2XHM; X-ray; 1.96 A; A=17-614.
PDB; 3ZQZ; X-ray; 2.35 A; A=17-614.
PDB; 4AA1; X-ray; 1.99 A; A=17-614.
PDB; 4AA2; X-ray; 1.99 A; A=17-614.
PDB; 4ASQ; X-ray; 1.99 A; A=17-614.
PDB; 4ASR; X-ray; 1.90 A; A=17-614.
PDB; 4CA7; X-ray; 1.82 A; A=17-614.
PDB; 4CA8; X-ray; 1.99 A; A=17-614.
PDB; 5A2R; X-ray; 1.85 A; A=18-615.
PDBsum; 1J36; -.
PDBsum; 1J37; -.
PDBsum; 1J38; -.
PDBsum; 2X8Y; -.
PDBsum; 2X8Z; -.
PDBsum; 2X90; -.
PDBsum; 2X91; -.
PDBsum; 2X92; -.
PDBsum; 2X93; -.
PDBsum; 2X94; -.
PDBsum; 2X95; -.
PDBsum; 2X96; -.
PDBsum; 2X97; -.
PDBsum; 2XHM; -.
PDBsum; 3ZQZ; -.
PDBsum; 4AA1; -.
PDBsum; 4AA2; -.
PDBsum; 4ASQ; -.
PDBsum; 4ASR; -.
PDBsum; 4CA7; -.
PDBsum; 4CA8; -.
PDBsum; 5A2R; -.
ProteinModelPortal; Q10714; -.
SMR; Q10714; -.
BioGrid; 60835; 2.
IntAct; Q10714; 7.
MINT; MINT-808657; -.
STRING; 7227.FBpp0080129; -.
MEROPS; M02.003; -.
iPTMnet; Q10714; -.
PaxDb; Q10714; -.
PRIDE; Q10714; -.
EnsemblMetazoa; FBtr0080552; FBpp0080129; FBgn0012037.
EnsemblMetazoa; FBtr0080553; FBpp0080130; FBgn0012037.
EnsemblMetazoa; FBtr0343667; FBpp0310259; FBgn0012037.
GeneID; 34805; -.
KEGG; dme:Dmel_CG8827; -.
CTD; 34805; -.
FlyBase; FBgn0012037; Ance.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
InParanoid; Q10714; -.
KO; K01283; -.
OMA; GPCLPLE; -.
OrthoDB; EOG091G033S; -.
PhylomeDB; Q10714; -.
BRENDA; 3.4.15.1; 1994.
SABIO-RK; Q10714; -.
EvolutionaryTrace; Q10714; -.
GenomeRNAi; 34805; -.
PRO; PR:Q10714; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0012037; -.
ExpressionAtlas; Q10714; differential.
Genevisible; Q10714; DM.
GO; GO:0005615; C:extracellular space; IDA:FlyBase.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:FlyBase.
GO; GO:0007552; P:metamorphosis; IEP:FlyBase.
GO; GO:0006508; P:proteolysis; IDA:FlyBase.
GO; GO:0009609; P:response to symbiotic bacterium; IMP:FlyBase.
GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
GO; GO:0007289; P:spermatid nucleus differentiation; IMP:FlyBase.
CDD; cd06461; M2_ACE; 1.
InterPro; IPR001548; Peptidase_M2.
PANTHER; PTHR10514; PTHR10514; 1.
Pfam; PF01401; Peptidase_M2; 1.
PRINTS; PR00791; PEPDIPTASEA.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Carboxypeptidase; Complete proteome; Disulfide bond;
Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
Reference proteome; Secreted; Signal; Zinc.
SIGNAL 1 17
CHAIN 18 615 Angiotensin-converting enzyme.
/FTId=PRO_0000028563.
ACT_SITE 368 368
METAL 367 367 Zinc; catalytic.
METAL 371 371 Zinc; catalytic.
METAL 395 395 Zinc; catalytic.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:8761461}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:8761461}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:8761461}.
DISULFID 133 141
DISULFID 336 354
DISULFID 467 612
DISULFID 522 540
CONFLICT 48 51 WAYG -> GPMR (in Ref. 4; AAC46902).
{ECO:0000305}.
CONFLICT 141 141 C -> S (in Ref. 4; AAC46902).
{ECO:0000305}.
CONFLICT 293 293 G -> A (in Ref. 2; AAB02171).
{ECO:0000305}.
CONFLICT 346 346 T -> I (in Ref. 1, 2; AAB02171, 4;
AAC46902 and 5). {ECO:0000305}.
CONFLICT 365 365 V -> E (in Ref. 1). {ECO:0000305}.
CONFLICT 402 402 S -> A (in Ref. 1). {ECO:0000305}.
CONFLICT 414 414 I -> T (in Ref. 1). {ECO:0000305}.
CONFLICT 486 486 S -> T (in Ref. 4; AAC46902).
{ECO:0000305}.
CONFLICT 533 533 V -> M (in Ref. 4; AAC46902).
{ECO:0000305}.
CONFLICT 547 547 A -> R (in Ref. 2; AAB02171).
{ECO:0000305}.
HELIX 20 22 {ECO:0000244|PDB:4CA7}.
HELIX 26 51 {ECO:0000244|PDB:4CA7}.
HELIX 56 80 {ECO:0000244|PDB:4CA7}.
HELIX 85 87 {ECO:0000244|PDB:4CA7}.
HELIX 91 101 {ECO:0000244|PDB:4CA7}.
HELIX 104 107 {ECO:0000244|PDB:4CA7}.
HELIX 110 129 {ECO:0000244|PDB:4CA7}.
TURN 145 147 {ECO:0000244|PDB:4CA7}.
HELIX 148 155 {ECO:0000244|PDB:4CA7}.
HELIX 159 173 {ECO:0000244|PDB:4CA7}.
HELIX 175 177 {ECO:0000244|PDB:4CA7}.
HELIX 178 194 {ECO:0000244|PDB:4CA7}.
HELIX 200 205 {ECO:0000244|PDB:4CA7}.
HELIX 206 208 {ECO:0000244|PDB:4CA7}.
HELIX 213 243 {ECO:0000244|PDB:4CA7}.
TURN 245 247 {ECO:0000244|PDB:4CA7}.
STRAND 250 252 {ECO:0000244|PDB:4CA7}.
HELIX 256 258 {ECO:0000244|PDB:4CA7}.
STRAND 259 261 {ECO:0000244|PDB:4CA7}.
HELIX 268 270 {ECO:0000244|PDB:4CA7}.
HELIX 271 274 {ECO:0000244|PDB:4CA7}.
STRAND 278 280 {ECO:0000244|PDB:1J37}.
HELIX 286 291 {ECO:0000244|PDB:4CA7}.
HELIX 296 309 {ECO:0000244|PDB:4CA7}.
HELIX 317 322 {ECO:0000244|PDB:4CA7}.
STRAND 329 331 {ECO:0000244|PDB:2X96}.
STRAND 339 342 {ECO:0000244|PDB:4CA7}.
STRAND 344 347 {ECO:0000244|PDB:4CA7}.
STRAND 349 352 {ECO:0000244|PDB:4CA7}.
HELIX 359 377 {ECO:0000244|PDB:4CA7}.
TURN 378 380 {ECO:0000244|PDB:4CA7}.
HELIX 383 385 {ECO:0000244|PDB:4CA7}.
HELIX 391 405 {ECO:0000244|PDB:4CA7}.
HELIX 408 413 {ECO:0000244|PDB:4CA7}.
STRAND 416 419 {ECO:0000244|PDB:1J36}.
HELIX 424 438 {ECO:0000244|PDB:4CA7}.
HELIX 441 456 {ECO:0000244|PDB:4CA7}.
TURN 457 459 {ECO:0000244|PDB:1J37}.
HELIX 462 464 {ECO:0000244|PDB:4CA7}.
HELIX 465 477 {ECO:0000244|PDB:4CA7}.
HELIX 492 494 {ECO:0000244|PDB:4CA7}.
HELIX 496 499 {ECO:0000244|PDB:4CA7}.
HELIX 505 524 {ECO:0000244|PDB:4CA7}.
TURN 525 527 {ECO:0000244|PDB:1J37}.
STRAND 530 535 {ECO:0000244|PDB:1J37}.
HELIX 537 539 {ECO:0000244|PDB:4CA7}.
HELIX 546 556 {ECO:0000244|PDB:4CA7}.
TURN 557 560 {ECO:0000244|PDB:4CA7}.
HELIX 564 572 {ECO:0000244|PDB:4CA7}.
HELIX 580 599 {ECO:0000244|PDB:4CA7}.
STRAND 611 613 {ECO:0000244|PDB:4CA7}.
SEQUENCE 615 AA; 70914 MW; 9E3691BCC51D6C48 CRC64;
MRLFLLALLA TLAVTQALVK EEIQAKEYLE NLNKELAKRT NVETEAAWAY GSNITDENEK
KKNEISAELA KFMKEVASDT TKFQWRSYQS EDLKRQFKAL TKLGYAALPE DDYAELLDTL
SAMESNFAKV KVCDYKDSTK CDLALDPEIE EVISKSRDHE ELAYYWREFY DKAGTAVRSQ
FERYVELNTK AAKLNNFTSG AEAWLDEYED DTFEQQLEDI FADIRPLYQQ IHGYVRFRLR
KHYGDAVVSE TGPIPMHLLG NMWAQQWSEI ADIVSPFPEK PLVDVSAEME KQGYTPLKMF
QMGDDFFTSM NLTKLPQDFW DKSIIEKPTD GRDLVCHASA WDFYLTDDVR IKQCTRVTQD
QLFTVHHELG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV LSLSVSTPKH LEKIGLLKDY
VRDDEARINQ LFLTALDKIV FLPFAFTMDK YRWSLFRGEV DKANWNCAFW KLRDEYSGIE
PPVVRSEKDF DAPAKYHISA DVEYLRYLVS FIIQFQFYKS ACIKAGQYDP DNVELPLDNC
DIYGSAAAGA AFHNMLSMGA SKPWPDALEA FNGERIMSGK AIAEYFEPLR VWLEAENIKN
NVHIGWTTSN KCVSS


Related products :

Catalog number Product name Quantity
20-272-190613 Angiotensin Converting Enzyme - Mouse monoclonal [ 9B9] to Angiotensin Converting Enzyme; EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.5 ml
20-272-190609 Angiotensin Converting Enzyme - Mouse monoclonal [2E2] to Angiotensin Converting Enzyme; EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.5 ml
20-272-190612 Angiotensin Converting Enzyme - Mouse monoclonal [3C5] to Angiotensin Converting Enzyme; EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.5 ml
20-272-190610 Angiotensin Converting Enzyme ( Biotin ) - Mouse monoclonal [i2H5] to Angiotensin Converting Enzyme ( Biotin ); EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.05 mg
20-272-190611 Angiotensin Converting Enzyme ( FITC ) - Mouse monoclonal [i2H5] to Angiotensin Converting Enzyme ( FITC ); EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.05 mg
20-272-190598 Angiotensin Converting Enzyme ( FITC ) - Mouse monoclonal [ i1A8] to Angiotensin Converting Enzyme ( FITC ); EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.05 mg
E0004r ELISA ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Rat,Rattus norvegicus 96T
E0004m ELISA ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Mouse,Mus musculus 96T
E0004b ELISA ACE,ACE,Angiotensin-converting enzyme,Bos taurus,Bovine,DCP1,Dipeptidyl carboxypeptidase I,Kininase II 96T
E0004b ELISA kit ACE,ACE,Angiotensin-converting enzyme,Bos taurus,Bovine,DCP1,Dipeptidyl carboxypeptidase I,Kininase II 96T
E0004m ELISA kit ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Mouse,Mus musculus 96T
U0004b CLIA ACE,ACE,Angiotensin-converting enzyme,Bos taurus,Bovine,DCP1,Dipeptidyl carboxypeptidase I,Kininase II 96T
E0004r ELISA kit ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Rat,Rattus norvegicus 96T
U0004r CLIA ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Rat,Rattus norvegicus 96T
U0004m CLIA ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Mouse,Mus musculus 96T
20-272-190614 Angiotensin Converting Enzyme ( Biotin ) - Mouse monoclonal [9B9] to Angiotensin Converting Enzyme ( Biotin ); EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.05 mg
20-272-190615 Angiotensin Converting Enzyme ( FITC ) - Mouse monoclonal [9B9] to Angiotensin Converting Enzyme ( FITC ); EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.05 mg
U0004Rb CLIA ACE,ACE,Angiotensin-converting enzyme,DCP1,Dipeptidyl carboxypeptidase I,Kininase II,Oryctolagus cuniculus,Rabbit 96T
E0004Rb ELISA kit ACE,ACE,Angiotensin-converting enzyme,DCP1,Dipeptidyl carboxypeptidase I,Kininase II,Oryctolagus cuniculus,Rabbit 96T
E0004h ELISA ACE,ACE,Angiotensin-converting enzyme,DCP,DCP1,Dipeptidyl carboxypeptidase I,Homo sapiens,Human,Kininase II 96T
U0004h CLIA ACE,ACE,Angiotensin-converting enzyme,DCP,DCP1,Dipeptidyl carboxypeptidase I,Homo sapiens,Human,Kininase II 96T
E0004Rb ELISA ACE,ACE,Angiotensin-converting enzyme,DCP1,Dipeptidyl carboxypeptidase I,Kininase II,Oryctolagus cuniculus,Rabbit 96T
E0004h ELISA kit ACE,ACE,Angiotensin-converting enzyme,DCP,DCP1,Dipeptidyl carboxypeptidase I,Homo sapiens,Human,Kininase II 96T
E0004c ELISA kit ACE,ACE,Angiotensin-converting enzyme,Chicken,DCP1,Dipeptidyl carboxypeptidase I,Gallus gallus,Kininase II 96T
E0004c ELISA ACE,ACE,Angiotensin-converting enzyme,Chicken,DCP1,Dipeptidyl carboxypeptidase I,Gallus gallus,Kininase II 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 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