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Molybdopterin synthase catalytic subunit (EC 2.8.1.12) (MOCO1-B) (Molybdenum cofactor synthesis protein 2 large subunit) (Molybdenum cofactor synthesis protein 2B) (MOCS2B) (Molybdopterin-synthase large subunit) (MPT synthase large subunit)

 MOC2B_HUMAN             Reviewed;         188 AA.
O96007; Q6IAI3;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
20-JUN-2018, entry version 146.
RecName: Full=Molybdopterin synthase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_03052};
EC=2.8.1.12 {ECO:0000255|HAMAP-Rule:MF_03052};
AltName: Full=MOCO1-B;
AltName: Full=Molybdenum cofactor synthesis protein 2 large subunit {ECO:0000255|HAMAP-Rule:MF_03052};
AltName: Full=Molybdenum cofactor synthesis protein 2B {ECO:0000255|HAMAP-Rule:MF_03052};
Short=MOCS2B {ECO:0000255|HAMAP-Rule:MF_03052};
AltName: Full=Molybdopterin-synthase large subunit;
Short=MPT synthase large subunit;
Name=MOCS2 {ECO:0000255|HAMAP-Rule:MF_03052}; Synonyms=MCBPE, MOCO1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF BICISTRONIC GENE, AND
TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10053003; DOI=10.1086/302295;
Stallmeyer B., Drugeon G., Reiss J., Haenni A.L., Mendel R.R.;
"Human molybdopterin synthase gene: identification of a bicistronic
transcript with overlapping reading frames.";
Am. J. Hum. Genet. 64:698-705(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9889283; DOI=10.1093/nar/27.3.854;
Sloan J., Kinghorn J.R., Unkles S.E.;
"The two subunits of human molybdopterin synthase: evidence for a
bicistronic messenger RNA with overlapping reading frames.";
Nucleic Acids Res. 27:854-858(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adrenal gland;
Huang C., Huang Q., Wu T., Peng Y., Gu Y., Zhang L., Jiang C., Li Y.,
Han Z., Wang Y., Chen Z., Fu G.;
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Duodenum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
ENZYME ACTIVITY, FUNCTION, AND SUBUNIT.
PubMed=12732628; DOI=10.1074/jbc.M303092200;
Leimkuehler S., Freuer A., Araujo J.A., Rajagopalan K.V., Mendel R.R.;
"Mechanistic studies of human molybdopterin synthase reaction and
characterization of mutants identified in group B patients of
molybdenum cofactor deficiency.";
J. Biol. Chem. 278:26127-26134(2003).
[9]
ENZYME ACTIVITY, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15073332; DOI=10.1073/pnas.0308191101;
Matthies A., Rajagopalan K.V., Mendel R.R., Leimkuehler S.;
"Evidence for the physiological role of a rhodanese-like protein for
the biosynthesis of the molybdenum cofactor in humans.";
Proc. Natl. Acad. Sci. U.S.A. 101:5946-5951(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
VARIANT MOCODB LYS-168.
PubMed=10053004; DOI=10.1086/302296;
Reiss J., Dorche C., Stallmeyer B., Mendel R.R., Cohen N.,
Zabot M.-T.;
"Human molybdopterin synthase gene: genomic structure and mutations in
molybdenum cofactor deficiency type B.";
Am. J. Hum. Genet. 64:706-711(1999).
[19]
INVOLVEMENT IN MOCODB.
PubMed=16021469; DOI=10.1007/s00439-005-1341-9;
Leimkuehler S., Charcosset M., Latour P., Dorche C., Kleppe S.,
Scaglia F., Szymczak I., Schupp P., Hahnewald R., Reiss J.;
"Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2
and in vitro characterization of a MOCS2 mutation that abolishes the
binding ability of molybdopterin synthase.";
Hum. Genet. 117:565-570(2005).
[20]
INVOLVEMENT IN MOCODB.
PubMed=16737835; DOI=10.1016/j.ymgme.2006.04.008;
Hahnewald R., Leimkuehler S., Vilaseca A., Acquaviva-Bourdain C.,
Lenz U., Reiss J.;
"A novel MOCS2 mutation reveals coordinated expression of the small
and large subunit of molybdopterin synthase.";
Mol. Genet. Metab. 89:210-213(2006).
-!- FUNCTION: Catalytic subunit of the molybdopterin synthase complex,
a complex that catalyzes the conversion of precursor Z into
molybdopterin. Acts by mediating the incorporation of 2 sulfur
atoms from thiocarboxylated MOCS2A into precursor Z to generate a
dithiolene group. {ECO:0000255|HAMAP-Rule:MF_03052,
ECO:0000269|PubMed:12732628, ECO:0000269|PubMed:15073332}.
-!- CATALYTIC ACTIVITY: Cyclic pyranopterin phosphate + 2
[molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-
C(O)SH + H(2)O = molybdopterin + 2 [molybdopterin-synthase sulfur-
carrier protein]. {ECO:0000255|HAMAP-Rule:MF_03052,
ECO:0000269|PubMed:12732628, ECO:0000269|PubMed:15073332}.
-!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_03052}.
-!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
(MOCS2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03052}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
Rule:MF_03052, ECO:0000269|PubMed:15073332}.
-!- TISSUE SPECIFICITY: Highest levels are found in heart and skeletal
muscle. Lower levels are present in brain, kidney and pancreas.
Very low levels are found in lung and peripheral blood leukocytes.
{ECO:0000269|PubMed:10053003}.
-!- DISEASE: Molybdenum cofactor deficiency, complementation group B
(MOCODB) [MIM:252160]: An autosomal recessive metabolic disorder
characterized by neonatal onset of intractable seizures,
opisthotonus, and facial dysmorphism associated with hypouricemia
and elevated urinary sulfite levels. Affected individuals show
severe neurologic damage and often die in early childhood.
{ECO:0000269|PubMed:10053004, ECO:0000269|PubMed:16021469,
ECO:0000269|PubMed:16737835}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: This protein is produced by a bicistronic gene
which also produces the small subunit (MOCS2A) from an overlapping
reading frame. Expression of these 2 proteins are related since a
mutation that removes the start codon of the small subunit
(MOCS2A) also impairs expression of the large subunit (MOCS2B).
-!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
{ECO:0000255|HAMAP-Rule:MF_03052}.
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EMBL; AF091871; AAD14599.1; -; mRNA.
EMBL; AF117815; AAD13297.1; -; mRNA.
EMBL; AF155659; AAF67478.1; -; mRNA.
EMBL; AK312887; BAG35735.1; -; mRNA.
EMBL; CR457172; CAG33453.1; -; mRNA.
EMBL; CH471123; EAW54874.1; -; Genomic_DNA.
EMBL; BC046097; AAH46097.1; -; mRNA.
CCDS; CCDS3958.1; -.
PIR; B59370; B59370.
RefSeq; NP_004522.1; NM_004531.4.
UniGene; Hs.163645; -.
UniGene; Hs.594335; -.
PDB; 4AP8; X-ray; 2.78 A; A/B/C/D=38-172.
PDB; 5MPO; X-ray; 2.43 A; C/D=27-179.
PDBsum; 4AP8; -.
PDBsum; 5MPO; -.
ProteinModelPortal; O96007; -.
SMR; O96007; -.
BioGrid; 110481; 5.
CORUM; O96007; -.
IntAct; O96007; 5.
STRING; 9606.ENSP00000380157; -.
iPTMnet; O96007; -.
PhosphoSitePlus; O96007; -.
BioMuta; MOCS2; -.
EPD; O96007; -.
MaxQB; O96007; -.
PaxDb; O96007; -.
PeptideAtlas; O96007; -.
PRIDE; O96007; -.
ProteomicsDB; 51186; -.
Ensembl; ENST00000396954; ENSP00000380157; ENSG00000164172.
GeneID; 4338; -.
KEGG; hsa:4338; -.
UCSC; uc003joz.5; human.
CTD; 4338; -.
DisGeNET; 4338; -.
EuPathDB; HostDB:ENSG00000164172.18; -.
GeneCards; MOCS2; -.
HGNC; HGNC:7193; MOCS2.
HPA; HPA037679; -.
HPA; HPA037680; -.
MalaCards; MOCS2; -.
MIM; 252160; phenotype.
MIM; 603708; gene.
neXtProt; NX_O96007; -.
OpenTargets; ENSG00000164172; -.
PharmGKB; PA30903; -.
eggNOG; KOG3307; Eukaryota.
eggNOG; COG0314; LUCA.
GeneTree; ENSGT00510000047669; -.
HOGENOM; HOG000280991; -.
InParanoid; O96007; -.
KO; K03635; -.
OMA; WKKEMYE; -.
OrthoDB; EOG091G0CV5; -.
PhylomeDB; O96007; -.
TreeFam; TF314334; -.
BioCyc; MetaCyc:HS09033-MONOMER; -.
BRENDA; 2.8.1.12; 2681.
Reactome; R-HSA-947581; Molybdenum cofactor biosynthesis.
UniPathway; UPA00344; -.
ChiTaRS; MOCS2; human.
GeneWiki; MOCS2; -.
GenomeRNAi; 4338; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000164172; -.
CleanEx; HS_MOCS2; -.
ExpressionAtlas; O96007; baseline and differential.
Genevisible; O96007; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0019008; C:molybdopterin synthase complex; IPI:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0030366; F:molybdopterin synthase activity; IDA:UniProtKB.
GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:UniProtKB.
GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central.
CDD; cd00756; MoaE; 1.
Gene3D; 3.90.1170.40; -; 1.
HAMAP; MF_03052; MOC2B; 1.
InterPro; IPR036563; MoaE_sf.
InterPro; IPR028888; MOCS2B_euk.
InterPro; IPR003448; Mopterin_biosynth_MoaE.
Pfam; PF02391; MoaE; 1.
SUPFAM; SSF54690; SSF54690; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Disease mutation;
Molybdenum cofactor biosynthesis; Phosphoprotein; Polymorphism;
Reference proteome; Transferase.
CHAIN 1 188 Molybdopterin synthase catalytic subunit.
/FTId=PRO_0000163111.
REGION 143 144 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03052}.
REGION 166 168 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03052}.
BINDING 159 159 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03052}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VARIANT 50 50 T -> A (in dbSNP:rs2233213).
/FTId=VAR_050091.
VARIANT 77 77 T -> A (in dbSNP:rs2233215).
/FTId=VAR_050092.
VARIANT 123 123 H -> Y (in dbSNP:rs2233218).
/FTId=VAR_050093.
VARIANT 168 168 E -> K (in MOCODB; dbSNP:rs121908605).
{ECO:0000269|PubMed:10053004}.
/FTId=VAR_012765.
VARIANT 187 187 N -> S (in dbSNP:rs2233221).
/FTId=VAR_050094.
STRAND 45 52 {ECO:0000244|PDB:5MPO}.
HELIX 56 63 {ECO:0000244|PDB:5MPO}.
STRAND 70 78 {ECO:0000244|PDB:5MPO}.
STRAND 80 82 {ECO:0000244|PDB:5MPO}.
STRAND 85 94 {ECO:0000244|PDB:5MPO}.
HELIX 98 113 {ECO:0000244|PDB:5MPO}.
STRAND 116 124 {ECO:0000244|PDB:5MPO}.
STRAND 126 130 {ECO:0000244|PDB:5MPO}.
STRAND 132 143 {ECO:0000244|PDB:5MPO}.
HELIX 144 161 {ECO:0000244|PDB:5MPO}.
STRAND 164 170 {ECO:0000244|PDB:5MPO}.
SEQUENCE 188 AA; 20944 MW; F405256D85621146 CRC64;
MSSLEISSSC FSLETKLPLS PPLVEDSAFE PSRKDMDEVE EKSKDVINFT AEKLSVDEVS
QLVISPLCGA ISLFVGTTRN NFEGKKVISL EYEAYLPMAE NEVRKICSDI RQKWPVKHIA
VFHRLGLVPV SEASIIIAVS SAHRAASLEA VSYAIDTLKA KVPIWKKEIY EESSTWKGNK
ECFWASNS


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EIAAB25089 Cell migration-inducing gene 11 protein,Homo sapiens,Human,MIG11,MOCS1,Molybdenum cofactor biosynthesis protein 1,Molybdenum cofactor synthesis-step 1 protein A-B
MOC2B_MOUSE ELISA Kit FOR Molybdopterin synthase catalytic subunit; organism: Mouse; gene name: Mocs2 96T
29-258 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.1 mg
27-880 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.1 mg
29-259 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.1 mg


 

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