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Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme (ATP:glutamine synthetase adenylyltransferase) (ATase) [Includes: Glutamine synthetase adenylyl-L-tyrosine phosphorylase (EC 2.7.7.89) (Adenylyl removase) (AR) (AT-N) (AT-N440) (P-I); Glutamine synthetase adenylyl transferase (EC 2.7.7.42) (Adenylyl transferase) (AT) (AT-C)]

 GLNE_ECOLI              Reviewed;         946 AA.
P30870; P78107; Q2M9F2;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
05-JUL-2017, entry version 128.
RecName: Full=Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme {ECO:0000305};
AltName: Full=ATP:glutamine synthetase adenylyltransferase {ECO:0000303|PubMed:4867671};
AltName: Full=ATase {ECO:0000303|PubMed:9312015};
Includes:
RecName: Full=Glutamine synthetase adenylyl-L-tyrosine phosphorylase {ECO:0000305|PubMed:4920873};
EC=2.7.7.89 {ECO:0000269|PubMed:4934180, ECO:0000305|PubMed:14766310, ECO:0000305|PubMed:4893578, ECO:0000305|PubMed:4920873, ECO:0000305|PubMed:9312015};
AltName: Full=Adenylyl removase {ECO:0000303|PubMed:20026075};
Short=AR {ECO:0000303|PubMed:20026075};
Short=AT-N {ECO:0000303|PubMed:9312015};
Short=AT-N440 {ECO:0000303|PubMed:14766310};
Short=P-I {ECO:0000303|PubMed:4934180};
Includes:
RecName: Full=Glutamine synthetase adenylyl transferase {ECO:0000303|PubMed:4920894};
EC=2.7.7.42 {ECO:0000269|PubMed:4920894, ECO:0000305|PubMed:9312015};
AltName: Full=Adenylyl transferase {ECO:0000303|PubMed:20026075};
Short=AT {ECO:0000303|PubMed:20026075};
Short=AT-C {ECO:0000303|PubMed:9312015};
Name=glnE {ECO:0000303|PubMed:8412694};
OrderedLocusNames=b3053, JW3025;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=K12 / CS520;
PubMed=8412694; DOI=10.1111/j.1365-2958.1993.tb01706.x;
van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.;
"The genes of the glutamine synthetase adenylylation cascade are not
regulated by nitrogen in Escherichia coli.";
Mol. Microbiol. 9:443-458(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
FUNCTION, ENZYME REGULATION, AND COFACTOR.
PubMed=4867671; DOI=10.1073/pnas.58.4.1703;
Kingdon H.S., Shapiro B.M., Stadtman E.R.;
"Regulation of glutamine synthetase. 8. ATP: glutamine synthetase
adenylyltransferase, an enzyme that catalyzes alterations in the
regulatory properties of glutamine synthetase.";
Proc. Natl. Acad. Sci. U.S.A. 58:1703-1710(1967).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
AND ENZYME REGULATION.
PubMed=4893578; DOI=10.1021/bi00830a030;
Shapiro B.M.;
"The glutamine synthetase deadenylylating enzyme system from
Escherichia coli. Resolution into two components, specific nucleotide
stimulation, and cofactor requirements.";
Biochemistry 8:659-670(1969).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=4920873; DOI=10.1016/0006-291X(70)90070-7;
Anderson W.B., Stadtman E.R.;
"Glutamine synthetase deadenylation: a phosphorolytic reaction
yielding ADP as nucleotide product.";
Biochem. Biophys. Res. Commun. 41:704-709(1970).
[7]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, AND SUBSTRATE SPECIFICITY.
PubMed=4920894; DOI=10.1111/j.1432-1033.1970.tb00320.x;
Ebner E., Wolf D., Gancedo C., Elsaesser S., Holzer H.;
"ATP: glutamine synthetase adenylyltransferase from Escherichia coli
B. Purification and properties.";
Eur. J. Biochem. 14:535-544(1970).
[8]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ENZYME REGULATION.
PubMed=4934180; DOI=10.1016/0003-9861(71)90229-3;
Anderson W.B., Stadtman E.R.;
"Purification and functional roles of the P I and P II components of
Escherichia coli glutamine synthetase deadenylylation system.";
Arch. Biochem. Biophys. 143:428-443(1971).
[9]
ENZYME REGULATION.
PubMed=33597; DOI=10.1016/0003-9861(78)90398-3;
Engleman E.G., Francis S.H.;
"Cascade control of E. coli glutamine synthetase. II. Metabolite
regulation of the enzymes in the cascade.";
Arch. Biochem. Biophys. 191:602-612(1978).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=9312015; DOI=10.1093/emboj/16.18.5562;
Jaggi R., van Heeswijk W.C., Westerhoff H.V., Ollis D.L.,
Vasudevan S.G.;
"The two opposing activities of adenylyl transferase reside in
distinct homologous domains, with intramolecular signal
transduction.";
EMBO J. 16:5562-5571(1997).
[11]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=14766310; DOI=10.1016/j.pep.2003.11.001;
Xu Y., Wen D., Clancy P., Carr P.D., Ollis D.L., Vasudevan S.G.;
"Expression, purification, crystallization, and preliminary X-ray
analysis of the N-terminal domain of Escherichia coli adenylyl
transferase.";
Protein Expr. Purif. 34:142-146(2004).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-440.
PubMed=15130478; DOI=10.1016/j.str.2004.02.029;
Xu Y., Zhang R., Joachimiak A., Carr P.D., Huber T., Vasudevan S.G.,
Ollis D.L.;
"Structure of the N-terminal domain of Escherichia coli glutamine
synthetase adenylyltransferase.";
Structure 12:861-869(2004).
[13]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 449-946.
PubMed=20026075; DOI=10.1016/j.jmb.2009.12.011;
Xu Y., Carr P.D., Vasudevan S.G., Ollis D.L.;
"Structure of the adenylylation domain of E. coli glutamine synthetase
adenylyl transferase: evidence for gene duplication and evolution of a
new active site.";
J. Mol. Biol. 396:773-784(2010).
-!- FUNCTION: Involved in the regulation of glutamine synthetase GlnA,
a key enzyme in the process to assimilate ammonia
(PubMed:8412694). When cellular nitrogen levels are high, the C-
terminal adenylyl transferase inactivates GlnA by covalent
transfer of an adenylyl group from ATP to 'Tyr-398' of GlnA, thus
reducing its activity (PubMed:4920894, PubMed:9312015).
Conversely, when nitrogen levels are low, the N-terminal adenylyl
removase (AR) activates GlnA by removing the adenylyl group by
phosphorolysis, increasing its activity (PubMed:4893578,
PubMed:4920873, PubMed:4934180, PubMed:9312015, PubMed:14766310).
The regulatory region of GlnE binds the signal transduction
protein PII (GlnB) which indicates the nitrogen status of the cell
(PubMed:8412694). {ECO:0000269|PubMed:14766310,
ECO:0000269|PubMed:4867671, ECO:0000269|PubMed:4893578,
ECO:0000269|PubMed:4920873, ECO:0000269|PubMed:4920894,
ECO:0000269|PubMed:4934180, ECO:0000269|PubMed:8412694,
ECO:0000269|PubMed:9312015}.
-!- CATALYTIC ACTIVITY: [Glutamine synthetase]-O(4)-(5'-adenylyl)-L-
tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP.
{ECO:0000269|PubMed:4934180, ECO:0000305|PubMed:14766310,
ECO:0000305|PubMed:4893578, ECO:0000305|PubMed:4920873,
ECO:0000305|PubMed:9312015}.
-!- CATALYTIC ACTIVITY: ATP + [glutamine synthetase]-L-tyrosine =
diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-
tyrosine. {ECO:0000269|PubMed:4920894,
ECO:0000305|PubMed:9312015}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:4867671,
ECO:0000269|PubMed:4893578, ECO:0000269|PubMed:4920894,
ECO:0000269|PubMed:4934180};
Note=Can also use Mn(2+). {ECO:0000269|PubMed:4867671,
ECO:0000269|PubMed:4893578, ECO:0000269|PubMed:4920894,
ECO:0000269|PubMed:4934180};
-!- ENZYME REGULATION: The adenylation activity is stimulated by
glutamine and PII (GlnB), and inhibited by 2-oxoglutarate
(PubMed:4867671, PubMed:4920894, PubMed:33597, PubMed:9312015).
Deadenylation activity is stimulated by PII-UMP (GlnB-UMP) and 2-
oxoglutarate, and inhibited by glutamine (PubMed:4893578,
PubMed:4934180, PubMed:33597, PubMed:9312015, PubMed:14766310).
{ECO:0000269|PubMed:14766310, ECO:0000269|PubMed:33597,
ECO:0000269|PubMed:4867671, ECO:0000269|PubMed:4893578,
ECO:0000269|PubMed:4920894, ECO:0000269|PubMed:4934180,
ECO:0000269|PubMed:9312015}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=4 uM for adenylyl {ECO:0000269|PubMed:4893578};
KM=5 uM for [L-glutamate:ammonia ligase (ADP-forming)]
{ECO:0000269|PubMed:4920894};
KM=150 uM for ATP {ECO:0000269|PubMed:4920894};
pH dependence:
Optimum pH is between 7.3 and 7.6 (PubMed:4893578,
PubMed:4920894). The enzyme is stable between pH 4 and 9
(PubMed:4920894). {ECO:0000269|PubMed:4893578,
ECO:0000269|PubMed:4920894};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:4920894}.
-!- SIMILARITY: Belongs to the GlnE family. {ECO:0000305}.
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EMBL; Z21844; CAA79892.1; -; Genomic_DNA.
EMBL; U00096; AAC76089.1; -; Genomic_DNA.
EMBL; AP009048; BAE77104.1; -; Genomic_DNA.
PIR; C65093; C65093.
RefSeq; NP_417525.1; NC_000913.3.
RefSeq; WP_001301081.1; NZ_LN832404.1.
PDB; 1V4A; X-ray; 2.00 A; A=1-440.
PDB; 3K7D; X-ray; 2.40 A; A/B=449-946.
PDBsum; 1V4A; -.
PDBsum; 3K7D; -.
ProteinModelPortal; P30870; -.
SMR; P30870; -.
BioGrid; 4261515; 4.
DIP; DIP-9780N; -.
IntAct; P30870; 2.
STRING; 316385.ECDH10B_3228; -.
PaxDb; P30870; -.
PRIDE; P30870; -.
EnsemblBacteria; AAC76089; AAC76089; b3053.
EnsemblBacteria; BAE77104; BAE77104; BAE77104.
GeneID; 947552; -.
KEGG; ecj:JW3025; -.
KEGG; eco:b3053; -.
PATRIC; fig|1411691.4.peg.3678; -.
EchoBASE; EB1559; -.
EcoGene; EG11602; glnE.
eggNOG; ENOG4105CE6; Bacteria.
eggNOG; COG1391; LUCA.
HOGENOM; HOG000256491; -.
InParanoid; P30870; -.
KO; K00982; -.
PhylomeDB; P30870; -.
BioCyc; EcoCyc:GLNE-MONOMER; -.
BioCyc; MetaCyc:GLNE-MONOMER; -.
BRENDA; 2.7.7.42; 2026.
EvolutionaryTrace; P30870; -.
PRO; PR:P30870; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
GO; GO:0000820; P:regulation of glutamine family amino acid metabolic process; IDA:UniProtKB.
HAMAP; MF_00802; GlnE; 1.
InterPro; IPR023057; GlnE.
InterPro; IPR005190; GlnE_rpt_dom.
InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
Pfam; PF08335; GlnD_UR_UTase; 2.
Pfam; PF03710; GlnE; 2.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Magnesium;
Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
Reference proteome; Transferase.
CHAIN 1 946 Bifunctional glutamine synthetase
adenylyltransferase/adenylyl-removing
enzyme.
/FTId=PRO_0000209244.
REGION 1 440 Adenylyl removase.
{ECO:0000305|PubMed:20026075}.
REGION 441 448 Linker. {ECO:0000305|PubMed:20026075}.
REGION 449 946 Adenylyl transferase.
{ECO:0000305|PubMed:20026075}.
CONFLICT 524 524 Missing (in Ref. 1; CAA79892).
{ECO:0000305}.
CONFLICT 624 625 QL -> PV (in Ref. 1; CAA79892).
{ECO:0000305}.
HELIX 6 16 {ECO:0000244|PDB:1V4A}.
HELIX 25 27 {ECO:0000244|PDB:1V4A}.
HELIX 30 38 {ECO:0000244|PDB:1V4A}.
HELIX 40 48 {ECO:0000244|PDB:1V4A}.
HELIX 51 58 {ECO:0000244|PDB:1V4A}.
HELIX 63 68 {ECO:0000244|PDB:1V4A}.
HELIX 69 76 {ECO:0000244|PDB:1V4A}.
TURN 77 79 {ECO:0000244|PDB:1V4A}.
HELIX 83 106 {ECO:0000244|PDB:1V4A}.
HELIX 112 141 {ECO:0000244|PDB:1V4A}.
STRAND 156 159 {ECO:0000244|PDB:1V4A}.
HELIX 161 164 {ECO:0000244|PDB:1V4A}.
STRAND 174 180 {ECO:0000244|PDB:1V4A}.
HELIX 195 211 {ECO:0000244|PDB:1V4A}.
HELIX 230 232 {ECO:0000244|PDB:1V4A}.
STRAND 235 238 {ECO:0000244|PDB:1V4A}.
HELIX 239 249 {ECO:0000244|PDB:1V4A}.
HELIX 252 258 {ECO:0000244|PDB:1V4A}.
STRAND 262 265 {ECO:0000244|PDB:1V4A}.
HELIX 270 283 {ECO:0000244|PDB:1V4A}.
HELIX 290 310 {ECO:0000244|PDB:1V4A}.
TURN 316 318 {ECO:0000244|PDB:1V4A}.
HELIX 323 337 {ECO:0000244|PDB:1V4A}.
TURN 338 340 {ECO:0000244|PDB:1V4A}.
HELIX 342 344 {ECO:0000244|PDB:1V4A}.
HELIX 349 358 {ECO:0000244|PDB:1V4A}.
HELIX 364 385 {ECO:0000244|PDB:1V4A}.
TURN 386 389 {ECO:0000244|PDB:1V4A}.
HELIX 399 408 {ECO:0000244|PDB:1V4A}.
HELIX 414 434 {ECO:0000244|PDB:1V4A}.
HELIX 450 457 {ECO:0000244|PDB:3K7D}.
HELIX 459 461 {ECO:0000244|PDB:3K7D}.
HELIX 467 469 {ECO:0000244|PDB:3K7D}.
HELIX 474 493 {ECO:0000244|PDB:3K7D}.
HELIX 498 515 {ECO:0000244|PDB:3K7D}.
HELIX 521 535 {ECO:0000244|PDB:3K7D}.
HELIX 539 547 {ECO:0000244|PDB:3K7D}.
HELIX 549 561 {ECO:0000244|PDB:3K7D}.
HELIX 563 571 {ECO:0000244|PDB:3K7D}.
HELIX 573 580 {ECO:0000244|PDB:3K7D}.
HELIX 582 585 {ECO:0000244|PDB:3K7D}.
HELIX 594 601 {ECO:0000244|PDB:3K7D}.
TURN 602 604 {ECO:0000244|PDB:3K7D}.
HELIX 610 633 {ECO:0000244|PDB:3K7D}.
HELIX 639 641 {ECO:0000244|PDB:3K7D}.
HELIX 642 669 {ECO:0000244|PDB:3K7D}.
HELIX 673 675 {ECO:0000244|PDB:3K7D}.
STRAND 682 687 {ECO:0000244|PDB:3K7D}.
HELIX 689 692 {ECO:0000244|PDB:3K7D}.
STRAND 702 708 {ECO:0000244|PDB:3K7D}.
STRAND 715 720 {ECO:0000244|PDB:3K7D}.
HELIX 724 740 {ECO:0000244|PDB:3K7D}.
HELIX 759 761 {ECO:0000244|PDB:3K7D}.
STRAND 764 767 {ECO:0000244|PDB:3K7D}.
HELIX 768 777 {ECO:0000244|PDB:3K7D}.
HELIX 781 788 {ECO:0000244|PDB:3K7D}.
STRAND 791 794 {ECO:0000244|PDB:3K7D}.
HELIX 797 811 {ECO:0000244|PDB:3K7D}.
HELIX 817 834 {ECO:0000244|PDB:3K7D}.
STRAND 842 844 {ECO:0000244|PDB:3K7D}.
TURN 845 847 {ECO:0000244|PDB:3K7D}.
HELIX 852 866 {ECO:0000244|PDB:3K7D}.
TURN 867 869 {ECO:0000244|PDB:3K7D}.
HELIX 871 874 {ECO:0000244|PDB:3K7D}.
HELIX 879 888 {ECO:0000244|PDB:3K7D}.
HELIX 894 916 {ECO:0000244|PDB:3K7D}.
STRAND 921 924 {ECO:0000244|PDB:3K7D}.
TURN 925 928 {ECO:0000244|PDB:3K7D}.
HELIX 929 943 {ECO:0000244|PDB:3K7D}.
SEQUENCE 946 AA; 108418 MW; 6FD2D7BDC619DB83 CRC64;
MKPLSSPLQQ YWQTVVERLP EPLAEESLSA QAKSVLTFSD FVQDSVIAHP EWLTELESQP
PQADEWQHYA AWLQEALCNV SDEAGLMREL RLFRRRIMVR IAWAQTLALV TEESILQQLS
YLAETLIVAA RDWLYDACCR EWGTPCNAQG EAQPLLILGM GKLGGGELNF SSDIDLIFAW
PEHGCTQGGR RELDNAQFFT RMGQRLIKVL DQPTQDGFVY RVDMRLRPFG ESGPLVLSFA
ALEDYYQEQG RDWERYAMVK ARIMGDSEGV YANELRAMLR PFVFRRYIDF SVIQSLRNMK
GMIAREVRRR GLTDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLSAIAELH
LLSENDAEQL RVAYLFLRRL ENLLQSINDE QTQTLPSDEL NRARLAWAMD FADWPQLTGA
LTAHMTNVRR VFNELIGDDE SETQEESLSE QWRELWQDAL QEDDTTPVLA HLSEDDRKQV
LTLIADFRKE LDKRTIGPRG RQVLDHLMPH LLSDVCARED AAVTLSRITA LLVGIVTRTT
YLELLSEFPA ALKHLISLCA ASPMIASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ
YLLRVPEDDE EQQLEALRQF KQAQLLRIAA ADIAGTLPVM KVSDHLTWLA EAMIDAVVQQ
AWVQMVARYG KPNHLNEREG RGFAVVGYGK LGGWELGYSS DLDLIFLHDC PMDAMTDGER
EIDGRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGA AGMLVTSAEA FADYQKNEAW
TWEHQALVRA RVVYGDPQLT AHFDAVRREI MTLPREGKTL QTEVREMREK MRAHLGNKHR
DRFDIKADEG GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMEEQEAMAL
TRAYTTLRDE LHHLALQELP GHVSEDCFTA ERELVRASWQ KWLVEE


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E1348h ELISA kit ADCY10,Adenylate cyclase homolog,Adenylate cyclase type 10,AH-related protein,Germ cell soluble adenylyl cyclase,Homo sapiens,hsAC,Human,sAC,SAC,Testicular soluble adenylyl cyclase 96T
U1348h CLIA ADCY10,Adenylate cyclase homolog,Adenylate cyclase type 10,AH-related protein,Germ cell soluble adenylyl cyclase,Homo sapiens,hsAC,Human,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1349h ELISA kit ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Homo sapiens,Human 96T
E1349h ELISA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Homo sapiens,Human 96T
U1349h CLIA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Homo sapiens,Human 96T
E1349b ELISA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Bos taurus,Bovine,Ca(2+)_calmodulin-activated adenylyl cyclase 96T


 

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