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Cysteine synthase, mitochondrial (EC 2.5.1.47) (Beta-substituted Ala synthase 2;2) (ARAth-Bsas2;2) (CSase C) (AtCS-C) (CS-C) (O-acetylserine (thiol)-lyase) (O-acetylserine sulfhydrylase) (OAS-TL C)

 CYSKM_ARATH             Reviewed;         430 AA.
Q43725; Q8L4A2; Q9M1Z8; Q9M440;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
16-JAN-2004, sequence version 3.
23-MAY-2018, entry version 153.
RecName: Full=Cysteine synthase, mitochondrial;
EC=2.5.1.47;
AltName: Full=Beta-substituted Ala synthase 2;2;
Short=ARAth-Bsas2;2;
AltName: Full=CSase C;
Short=AtCS-C;
Short=CS-C;
AltName: Full=O-acetylserine (thiol)-lyase;
AltName: Full=O-acetylserine sulfhydrylase;
AltName: Full=OAS-TL C;
Flags: Precursor;
Name=OASC; Synonyms=ACS 1; OrderedLocusNames=At3g59760;
ORFNames=F24G16.30;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Flower;
PubMed=10319184; DOI=10.1007/BF01321531;
Hesse H., Lipke J., Altmann T., Hofgen R.;
"Molecular cloning and expression analyses of mitochondrial and
plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase)
from Arabidopsis thaliana.";
Amino Acids 16:113-131(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 43-430, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND INTERACTION WITH SAT3.
STRAIN=cv. Columbia;
PubMed=10940562; DOI=10.1016/S0378-1119(00)00261-4;
Jost R., Berkowitz O., Wirtz M., Hopkins L., Hawkesford M.J., Hell R.;
"Genomic and functional characterization of the oas gene family
encoding O-acetylserine (thiol) lyases, enzymes catalyzing the final
step in cysteine biosynthesis in Arabidopsis thaliana.";
Gene 253:237-247(2000).
[6]
NOMENCLATURE.
PubMed=10889265; DOI=10.1104/pp.123.3.1163;
Hatzfeld Y., Maruyama A., Schmidt A., Noji M., Ishizawa K., Saito K.;
"beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like
protein in spinach and Arabidopsis.";
Plant Physiol. 123:1163-1171(2000).
[7]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15258168; DOI=10.1093/jxb/erh201;
Wirtz M., Droux M., Hell R.;
"O-acetylserine (thiol) lyase: an enigmatic enzyme of plant cysteine
biosynthesis revisited in Arabidopsis thaliana.";
J. Exp. Bot. 55:1785-1798(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=14671022; DOI=10.1105/tpc.016055;
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome
highlights signaling and regulatory components, provides assessment of
targeting prediction programs, and indicates plant-specific
mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[9]
REVIEW.
PubMed=16307301; DOI=10.1007/s11120-005-8810-9;
Wirtz M., Droux M.;
"Synthesis of the sulfur amino acids: cysteine and methionine.";
Photosyn. Res. 86:345-362(2005).
[10]
FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18223034; DOI=10.1105/tpc.107.056747;
Heeg C., Kruse C., Jost R., Gutensohn M., Ruppert T., Wirtz M.,
Hell R.;
"Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family
demonstrates compartment-specific differences in the regulation of
cysteine synthesis.";
Plant Cell 20:168-185(2008).
[11]
GENE FAMILY, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18024555; DOI=10.1104/pp.107.106831;
Watanabe M., Kusano M., Oikawa A., Fukushima A., Noji M., Saito K.;
"Physiological roles of the beta-substituted alanine synthase gene
family in Arabidopsis.";
Plant Physiol. 146:310-320(2008).
[12]
COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
PubMed=18801369; DOI=10.1016/j.jmb.2008.08.075;
Feldman-Salit A., Wirtz M., Hell R., Wade R.C.;
"A mechanistic model of the cysteine synthase complex.";
J. Mol. Biol. 386:37-59(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20658158; DOI=10.1007/s00726-010-0694-0;
Wirtz M., Heeg C., Samami A.A., Ruppert T., Hell R.;
"Enzymes of cysteine synthesis show extensive and conserved
modifications patterns that include N(alpha)-terminal acetylation.";
Amino Acids 39:1077-1086(2010).
[14]
COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
PubMed=20720017; DOI=10.1074/jbc.M110.157446;
Wirtz M., Birke H., Heeg C., Mueller C., Hosp F., Throm C., Koenig S.,
Feldman-Salit A., Rippe K., Petersen G., Wade R.C., Rybin V.,
Scheffzek K., Hell R.;
"Structure and function of the hetero-oligomeric cysteine synthase
complex in plants.";
J. Biol. Chem. 285:32810-32817(2010).
[15]
INTERACTION WITH SAT3, AND COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
PubMed=22730323; DOI=10.1074/jbc.M112.372656;
Wirtz M., Beard K.F., Lee C.P., Boltz A., Schwarzlaender M., Fuchs C.,
Meyer A.J., Heeg C., Sweetlove L.J., Ratcliffe R.G., Hell R.;
"Mitochondrial cysteine synthase complex regulates O-acetylserine
biosynthesis in plants.";
J. Biol. Chem. 287:27941-27947(2012).
[16]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22511607; DOI=10.1093/mp/sss043;
Alvarez C., Garcia I., Romero L.C., Gotor C.;
"Mitochondrial sulfide detoxification requires a functional isoform O-
acetylserine(thiol)lyase C in Arabidopsis thaliana.";
Mol. Plant 5:1217-1226(2012).
[17]
INTERACTION WITH SAT3.
PubMed=23602110; DOI=10.1016/j.plantsci.2013.02.016;
Wawrzynska A., Kurzyk A., Mierzwinska M., Plochocka D., Wieczorek G.,
Sirko A.;
"Direct targeting of Arabidopsis cysteine synthase complexes with
synthetic polypeptides to selectively deregulate cysteine synthesis.";
Plant Sci. 207:148-157(2013).
[18]
IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE
AFTER PHE-87.
PubMed=25732537; DOI=10.1093/jxb/erv064;
Carrie C., Venne A.S., Zahedi R.P., Soll J.;
"Identification of cleavage sites and substrate proteins for two
mitochondrial intermediate peptidases in Arabidopsis thaliana.";
J. Exp. Bot. 66:2691-2708(2015).
-!- FUNCTION: Acts as a cysteine synthase. Plays a role in the sulfide
detoxification in mitochondria. {ECO:0000269|PubMed:18024555,
ECO:0000269|PubMed:18223034, ECO:0000269|PubMed:22511607}.
-!- CATALYTIC ACTIVITY: O-acetyl-L-serine + hydrogen sulfide = L-
cysteine + acetate. {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.98 mM for O(3)-acetyl-L-serine for the cysteine synthase
activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168};
KM=0.43 mM for O(3)-acetyl-L-serine for the cysteine synthase
activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168};
KM=4.7 uM for H(2)S for the cysteine synthase activity
{ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
Vmax=159 umol/min/mg enzyme for L-cysteine for the cysteine
synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168};
Vmax=534 umol/min/mg enzyme for L-cysteine for the cysteine
synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168};
Vmax=0.33 umol/min/mg enzyme for H(2)S for the L-3-cyanoalanine
synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168};
-!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
cysteine from L-serine: step 2/2.
-!- SUBUNIT: Homodimer (By similarity). Interacts with SAT3. Component
of the cysteine synthase complex (CSC) composed of two OAS-TL
dimers and one SAT hexamer. {ECO:0000250,
ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:22730323,
ECO:0000269|PubMed:23602110}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1633616, EBI-1633616;
Q39218:SAT3; NbExp=6; IntAct=EBI-1633616, EBI-1633440;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022,
ECO:0000305|PubMed:25732537}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q43725-1; Sequence=Displayed;
-!- DISRUPTION PHENOTYPE: No visible phenotype but displays lower
levels of thiols in roots (PubMed:18024555). Growth retardation
(PubMed:18223034). Defects in root hair formation
(PubMed:22511607). {ECO:0000269|PubMed:18024555,
ECO:0000269|PubMed:18223034, ECO:0000269|PubMed:22511607}.
-!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
synthase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA57498.1; Type=Frameshift; Positions=5, 424, 426; Evidence={ECO:0000305};
Sequence=CAB75795.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X81973; CAA57498.1; ALT_FRAME; mRNA.
EMBL; AL138647; CAB75795.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE79963.1; -; Genomic_DNA.
EMBL; AY099721; AAM20572.1; -; mRNA.
EMBL; AY128885; AAM91285.1; -; mRNA.
EMBL; AJ271727; CAB71290.1; -; mRNA.
PIR; T47800; T47800.
PIR; T52650; T52650.
RefSeq; NP_191535.2; NM_115838.6. [Q43725-1]
UniGene; At.25336; -.
PDB; 4AEC; X-ray; 2.40 A; A/B=1-430.
PDBsum; 4AEC; -.
ProteinModelPortal; Q43725; -.
SMR; Q43725; -.
BioGrid; 10459; 4.
DIP; DIP-40500N; -.
IntAct; Q43725; 3.
STRING; 3702.AT3G59760.1; -.
SwissPalm; Q43725; -.
PaxDb; Q43725; -.
PRIDE; Q43725; -.
EnsemblPlants; AT3G59760.3; AT3G59760.3; AT3G59760. [Q43725-1]
GeneID; 825145; -.
Gramene; AT3G59760.3; AT3G59760.3; AT3G59760. [Q43725-1]
KEGG; ath:AT3G59760; -.
Araport; AT3G59760; -.
eggNOG; KOG1252; Eukaryota.
eggNOG; COG0031; LUCA.
HOGENOM; HOG000217394; -.
InParanoid; Q43725; -.
KO; K01738; -.
PhylomeDB; Q43725; -.
BioCyc; MetaCyc:AT3G59760-MONOMER; -.
Reactome; R-ATH-1614603; Cysteine formation from homocysteine.
UniPathway; UPA00136; UER00200.
PRO; PR:Q43725; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q43725; baseline and differential.
Genevisible; Q43725; AT.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
InterPro; IPR005856; Cys_synth.
InterPro; IPR005859; CysK.
InterPro; IPR001216; P-phosphate_BS.
InterPro; IPR001926; PLP-dep.
InterPro; IPR036052; Trypto_synt_PLP_dependent.
Pfam; PF00291; PALP; 1.
SUPFAM; SSF53686; SSF53686; 1.
TIGRFAMs; TIGR01139; cysK; 1.
TIGRFAMs; TIGR01136; cysKM; 1.
PROSITE; PS00901; CYS_SYNTHASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amino-acid biosynthesis;
Complete proteome; Cysteine biosynthesis; Mitochondrion;
Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
TRANSIT 1 87 Mitochondrion.
{ECO:0000269|PubMed:25732537}.
CHAIN 88 430 Cysteine synthase, mitochondrial.
/FTId=PRO_0000006353.
REGION 289 293 Pyridoxal phosphate binding.
{ECO:0000250}.
COMPBIAS 49 54 Poly-Ser.
COMPBIAS 380 385 Poly-Ala.
BINDING 185 185 Pyridoxal phosphate. {ECO:0000250}.
BINDING 377 377 Pyridoxal phosphate. {ECO:0000250}.
MOD_RES 154 154 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
CONFLICT 49 49 Missing (in Ref. 1; CAA57498 and 5;
CAB71290). {ECO:0000305}.
CONFLICT 73 73 A -> G (in Ref. 1; CAA57498).
{ECO:0000305}.
CONFLICT 195 195 Missing (in Ref. 1; CAA57498).
{ECO:0000305}.
CONFLICT 314 314 E -> R (in Ref. 1; CAA57498).
{ECO:0000305}.
CONFLICT 356 357 SE -> ISKL (in Ref. 1; CAA57498).
{ECO:0000305}.
CONFLICT 385 385 Missing (in Ref. 1; CAA57498).
{ECO:0000305}.
CONFLICT 409 409 Missing (in Ref. 1; CAA57498).
{ECO:0000305}.
STRAND 114 116 {ECO:0000244|PDB:4AEC}.
HELIX 117 120 {ECO:0000244|PDB:4AEC}.
STRAND 126 128 {ECO:0000244|PDB:4AEC}.
HELIX 131 133 {ECO:0000244|PDB:4AEC}.
STRAND 137 144 {ECO:0000244|PDB:4AEC}.
HELIX 145 147 {ECO:0000244|PDB:4AEC}.
HELIX 155 167 {ECO:0000244|PDB:4AEC}.
TURN 173 175 {ECO:0000244|PDB:4AEC}.
STRAND 177 181 {ECO:0000244|PDB:4AEC}.
HELIX 185 197 {ECO:0000244|PDB:4AEC}.
STRAND 200 206 {ECO:0000244|PDB:4AEC}.
HELIX 211 219 {ECO:0000244|PDB:4AEC}.
STRAND 223 227 {ECO:0000244|PDB:4AEC}.
HELIX 229 231 {ECO:0000244|PDB:4AEC}.
HELIX 232 246 {ECO:0000244|PDB:4AEC}.
STRAND 250 252 {ECO:0000244|PDB:4AEC}.
TURN 255 257 {ECO:0000244|PDB:4AEC}.
HELIX 260 267 {ECO:0000244|PDB:4AEC}.
HELIX 269 276 {ECO:0000244|PDB:4AEC}.
STRAND 281 287 {ECO:0000244|PDB:4AEC}.
STRAND 289 291 {ECO:0000244|PDB:4AEC}.
HELIX 292 304 {ECO:0000244|PDB:4AEC}.
STRAND 308 315 {ECO:0000244|PDB:4AEC}.
HELIX 316 318 {ECO:0000244|PDB:4AEC}.
HELIX 320 322 {ECO:0000244|PDB:4AEC}.
TURN 345 347 {ECO:0000244|PDB:4AEC}.
STRAND 349 354 {ECO:0000244|PDB:4AEC}.
HELIX 356 370 {ECO:0000244|PDB:4AEC}.
HELIX 376 388 {ECO:0000244|PDB:4AEC}.
HELIX 392 394 {ECO:0000244|PDB:4AEC}.
STRAND 398 403 {ECO:0000244|PDB:4AEC}.
HELIX 407 410 {ECO:0000244|PDB:4AEC}.
HELIX 414 422 {ECO:0000244|PDB:4AEC}.
SEQUENCE 430 AA; 45815 MW; 9DDEB1B8E314E143 CRC64;
MVAMIMASRF NREAKLASQI LSTLLGNRSC YTSMAATSSS ALLLNPLTSS SSSSTLRRFR
CSPEISSLSF SSASDFSLAM KRQSRSFADG SERDPSVVCE AVKRETGPDG LNIADNVSQL
IGKTPMVYLN SIAKGCVANI AAKLEIMEPC CSVKDRIGYS MVTDAEQKGF ISPGKSVLVE
PTSGNTGIGL AFIAASRGYR LILTMPASMS MERRVLLKAF GAELVLTDPA KGMTGAVQKA
EEILKNTPDA YMLQQFDNPA NPKIHYETTG PEIWDDTKGK VDIFVAGIGT GGTITGVGRF
IKEKNPKTQV IGVEPTESDI LSGGKPGPHK IQGIGAGFIP KNLDQKIMDE VIAISSEEAI
ETAKQLALKE GLMVGISSGA AAAAAIKVAK RPENAGKLIA VVFPSFGERY LSTPLFQSIR
EEVEKMQPEV


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U2083b CLIA Bos taurus,Bovine,FECH,Ferrochelatase, mitochondrial,Heme synthase,Protoheme ferro-lyase 96T
U2083m CLIA Fech,Ferrochelatase, mitochondrial,Heme synthase,Mouse,Mus musculus,Protoheme ferro-lyase 96T
E2083h ELISA kit FECH,Ferrochelatase, mitochondrial,Heme synthase,Homo sapiens,Human,Protoheme ferro-lyase 96T
U2083h CLIA FECH,Ferrochelatase, mitochondrial,Heme synthase,Homo sapiens,Human,Protoheme ferro-lyase 96T
U2083h CLIA kit FECH,Ferrochelatase, mitochondrial,Heme synthase,Homo sapiens,Human,Protoheme ferro-lyase 96T
E2083h ELISA FECH,Ferrochelatase, mitochondrial,Heme synthase,Homo sapiens,Human,Protoheme ferro-lyase 96T


 

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