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Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) (ADP-glucose pyrophosphorylase) (ADPGlc PPase) (ADP-glucose synthase)

 GLGC_ECOLI              Reviewed;         431 AA.
P0A6V1; P00584; Q2M794;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 113.
RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000305};
EC=2.7.7.27 {ECO:0000269|PubMed:1648099};
AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000303|PubMed:826540};
Short=ADPGlc PPase {ECO:0000303|PubMed:21741429};
AltName: Full=ADP-glucose synthase {ECO:0000303|PubMed:2162151};
Name=glgC; OrderedLocusNames=b3430, JW3393;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6300111;
Baecker P.A., Furlong C.E., Preiss J.;
"Biosynthesis of bacterial glycogen. Primary structure of Escherichia
coli ADP-glucose synthetase as deduced from the nucleotide sequence of
the glg C gene.";
J. Biol. Chem. 258:5084-5088(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT CL1136.
STRAIN=B;
PubMed=1339262; DOI=10.1016/0003-9861(92)90553-9;
Ghosh P., Meyer C., Remy E., Peterson D., Preiss J.;
"Cloning, expression, and nucleotide sequence of glgC gene from an
allosteric mutant of Escherichia coli B.";
Arch. Biochem. Biophys. 296:122-128(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT SG5.
STRAIN=B;
PubMed=1320612; DOI=10.1128/jb.174.13.4509-4512.1992;
Meyer C.R., Ghosh P., Remy E., Preiss J.;
"Cloning, expression, and nucleotide sequence of a mutant glgC gene
from Escherichia coli B.";
J. Bacteriol. 174:4509-4512(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT SG14, AND SEQUENCE REVISION
TO 295.
STRAIN=B;
PubMed=8385906; DOI=10.1006/abbi.1993.1181;
Meyer C.R., Ghosh P., Nadler S., Preiss J.;
"Cloning, expression, and sequence of an allosteric mutant ADPglucose
pyrophosphorylase from Escherichia coli B.";
Arch. Biochem. Biophys. 302:64-71(1993).
[5]
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).
[6]
SEQUENCE REVISION TO 161; 166 AND 189, AND MUTANT 618.
PubMed=2543670;
Kumar A., Ghosh P., Lee Y.M., Hill M.A., Preiss J.;
"Biosynthesis of bacterial glycogen. Determination of the amino acid
changes that alter the regulatory properties of a mutant Escherichia
coli ADP-glucose synthetase.";
J. Biol. Chem. 264:10464-10471(1989).
[7]
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).
[8]
PROTEIN SEQUENCE OF 2-28, AND SUBUNIT.
PubMed=826540;
Haugen T.H., Ishaque A., Preiss J.;
"Biosynthesis of bacterial glycogen. Characterization of the subunit
structure of Escherichia coli B glucose-1-phosphate
adenylyltransferase (EC 2.7.7.27).";
J. Biol. Chem. 251:7880-7885(1976).
[9]
PROTEIN SEQUENCE OF 2-49 AND 183-201.
PubMed=359552;
Parsons T.F., Preiss J.;
"Biosynthesis of bacterial glycogen. Isolation and characterization of
the pyridoxal-P allosteric activator site and the ADP-glucose-
protected pyridoxal-P binding site of Escherichia coli B ADP-glucose
synthase.";
J. Biol. Chem. 253:7638-7645(1978).
[10]
MUTAGENESIS OF TYR-114.
PubMed=2844780;
Kumar A., Tanaka T., Lee Y.M., Preiss J.;
"Biosynthesis of bacterial glycogen. Use of site-directed mutagenesis
to probe the role of tyrosine 114 in the catalytic mechanism of ADP-
glucose synthetase from Escherichia coli.";
J. Biol. Chem. 263:14634-14639(1988).
[11]
ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-39.
PubMed=2162151; DOI=10.1016/0003-9861(90)90533-5;
Gardiol A., Preiss J.;
"Escherichia coli E-39 ADPglucose synthetase has different activation
kinetics from the wild-type allosteric enzyme.";
Arch. Biochem. Biophys. 280:175-180(1990).
[12]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
MUTAGENESIS OF LYS-195, AND ACTIVITY REGULATION.
STRAIN=K12;
PubMed=1648099;
Hill M.A., Kaufmann K., Otero J., Preiss J.;
"Biosynthesis of bacterial glycogen. Mutagenesis of a catalytic site
residue of ADP-glucose pyrophosphorylase from Escherichia coli.";
J. Biol. Chem. 266:12455-12460(1991).
[13]
INDUCTION.
STRAIN=K12 / BW3414;
PubMed=7751274; DOI=10.1128/jb.177.10.2663-2672.1995;
Liu M.Y., Yang H., Romeo T.;
"The product of the pleiotropic Escherichia coli gene csrA modulates
glycogen biosynthesis via effects on mRNA stability.";
J. Bacteriol. 177:2663-2672(1995).
[14]
ACTIVITY REGULATION, AND MUTAGENESIS OF GLN-74 AND TRP-113.
PubMed=21741429; DOI=10.1016/j.biochi.2011.06.029;
Figueroa C.M., Esper M.C., Bertolo A., Demonte A.M., Aleanzi M.,
Iglesias A.A., Ballicora M.A.;
"Understanding the allosteric trigger for the fructose-1,6-
bisphosphate regulation of the ADP-glucose pyrophosphorylase from
Escherichia coli.";
Biochimie 93:1816-1823(2011).
[15]
X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) IN COMPLEX WITH
FRUCTOSE-1,6-BISPHOSPHATE; AMP AND SUBSTRATE ANALOG, SUBUNIT, AND
REACTION MECHANISM.
PubMed=27545622; DOI=10.1016/j.str.2016.06.023;
Cifuente J.O., Comino N., Madariaga-Marcos J., Lopez-Fernandez S.,
Garcia-Alija M., Agirre J., Albesa-Jove D., Guerin M.E.;
"Structural basis of glycogen biosynthesis regulation in bacteria.";
Structure 24:1613-1622(2016).
-!- FUNCTION: Involved in the biosynthesis of ADP-glucose, a building
block required for the elongation reactions to produce glycogen.
Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate
(G1P) to produce pyrophosphate and ADP-Glc.
{ECO:0000269|PubMed:1648099}.
-!- CATALYTIC ACTIVITY: ATP + alpha-D-glucose 1-phosphate =
diphosphate + ADP-glucose. {ECO:0000269|PubMed:1648099}.
-!- ACTIVITY REGULATION: Allosterically activated by fructose-1,6-
bisphosphate (F16BP), hexanediol 1,6-bisphosphate, NADPH and
pyridoxal phosphate. Inhibited by AMP and by high concentrations
of MgCl(2). {ECO:0000269|PubMed:1648099,
ECO:0000269|PubMed:2162151, ECO:0000269|PubMed:21741429}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=25 uM for alpha-D-glucose 1-phosphate
{ECO:0000269|PubMed:1648099};
KM=120 uM for diphosphate {ECO:0000269|PubMed:1648099};
Vmax=133 umol/min/mg enzyme toward alpha-D-glucose 1-phosphate
{ECO:0000269|PubMed:1648099};
Vmax=97 umol/min/mg enzyme toward diphosphate
{ECO:0000269|PubMed:1648099};
Note=Kcat is 111 sec(-1) for adenylyltransferase activity. Kcat
is 81 sec(-1) for pyrophosphorylase activity.
{ECO:0000269|PubMed:1648099};
-!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
{ECO:0000305}.
-!- SUBUNIT: Homotetramer; dimer of dimers.
{ECO:0000269|PubMed:27545622, ECO:0000269|PubMed:826540}.
-!- INDUCTION: mRNA stability is at least partially under the control
of CsrA; loss of csrA leads to higher transcript levels, possibly
mediated by protein binding to the mRNA (PubMed:7751274).
{ECO:0000269|PubMed:7751274}.
-!- MISCELLANEOUS: Displays cooperative behavior and a bibi mechanism
with sequential binding of ATP and G1P, followed by ordered
release of pyrophosphate and ADP-Glc.
{ECO:0000269|PubMed:27545622}.
-!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
adenylyltransferase family. {ECO:0000305}.
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EMBL; V00281; CAA23544.1; -; Genomic_DNA.
EMBL; J01616; AAA98736.1; -; Genomic_DNA.
EMBL; M97226; AAA23873.1; -; Genomic_DNA.
EMBL; S58224; AAB26162.1; -; Genomic_DNA.
EMBL; U18997; AAA58228.1; -; Genomic_DNA.
EMBL; U00096; AAC76455.1; -; Genomic_DNA.
EMBL; AP009048; BAE77862.1; -; Genomic_DNA.
PIR; A00721; YUEC.
RefSeq; NP_417888.1; NC_000913.3.
RefSeq; WP_000253975.1; NZ_LN832404.1.
PDB; 5L6S; X-ray; 3.04 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-431.
PDB; 5L6V; X-ray; 2.67 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-431.
PDB; 5MNI; X-ray; 3.09 A; A/B/C/D/E/F/G/H=1-431.
PDBsum; 5L6S; -.
PDBsum; 5L6V; -.
PDBsum; 5MNI; -.
ProteinModelPortal; P0A6V1; -.
SMR; P0A6V1; -.
BioGrid; 4262502; 297.
DIP; DIP-48147N; -.
IntAct; P0A6V1; 6.
STRING; 316385.ECDH10B_3604; -.
EPD; P0A6V1; -.
PaxDb; P0A6V1; -.
PRIDE; P0A6V1; -.
EnsemblBacteria; AAC76455; AAC76455; b3430.
EnsemblBacteria; BAE77862; BAE77862; BAE77862.
GeneID; 947942; -.
KEGG; ecj:JW3393; -.
KEGG; eco:b3430; -.
PATRIC; fig|511145.12.peg.3527; -.
EchoBASE; EB0374; -.
EcoGene; EG10379; glgC.
eggNOG; ENOG4107QQ4; Bacteria.
eggNOG; COG0448; LUCA.
HOGENOM; HOG000278607; -.
InParanoid; P0A6V1; -.
KO; K00975; -.
OMA; HCVLGVR; -.
PhylomeDB; P0A6V1; -.
BioCyc; EcoCyc:GLUC1PADENYLTRANS-MONOMER; -.
BioCyc; MetaCyc:GLUC1PADENYLTRANS-MONOMER; -.
BRENDA; 2.7.7.27; 2026.
UniPathway; UPA00164; -.
PRO; PR:P0A6V1; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016208; F:AMP binding; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
GO; GO:0005978; P:glycogen biosynthetic process; IMP:EcoCyc.
GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
Gene3D; 3.90.550.10; -; 1.
HAMAP; MF_00624; GlgC; 1.
InterPro; IPR011831; ADP-Glc_PPase.
InterPro; IPR005836; ADP_Glu_pyroP_CS.
InterPro; IPR023049; GlgC_bac.
InterPro; IPR005835; NTP_transferase_dom.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR011004; Trimer_LpxA-like_sf.
Pfam; PF00483; NTP_transferase; 1.
SUPFAM; SSF51161; SSF51161; 1.
SUPFAM; SSF53448; SSF53448; 2.
TIGRFAMs; TIGR02091; glgC; 1.
PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; ATP-binding; Carbohydrate metabolism;
Complete proteome; Direct protein sequencing; Glycogen biosynthesis;
Glycogen metabolism; Nucleotide-binding; Nucleotidyltransferase;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:359552,
ECO:0000269|PubMed:826540}.
CHAIN 2 431 Glucose-1-phosphate adenylyltransferase.
/FTId=PRO_0000195294.
REGION 194 195 Alpha-D-glucose 1-phosphate binding.
{ECO:0000305|PubMed:1648099,
ECO:0000305|PubMed:27545622}.
REGION 419 423 Fructose-1,6-bisphosphate binding.
{ECO:0000269|PubMed:27545622}.
REGION 429 431 Fructose-1,6-bisphosphate binding.
{ECO:0000269|PubMed:27545622}.
BINDING 39 39 Fructose-1,6-bisphosphate.
{ECO:0000269|PubMed:27545622,
ECO:0000305|PubMed:2162151}.
BINDING 40 40 AMP. {ECO:0000269|PubMed:27545622}.
BINDING 46 46 AMP. {ECO:0000269|PubMed:27545622}.
BINDING 52 52 AMP. {ECO:0000269|PubMed:27545622}.
BINDING 114 114 Alpha-D-glucose 1-phosphate.
{ECO:0000305|PubMed:2844780}.
BINDING 130 130 AMP. {ECO:0000269|PubMed:27545622}.
BINDING 179 179 Alpha-D-glucose 1-phosphate; via amide
nitrogen. {ECO:0000305|PubMed:27545622}.
BINDING 212 212 Alpha-D-glucose 1-phosphate; via carbonyl
oxygen. {ECO:0000305|PubMed:27545622}.
BINDING 370 370 AMP. {ECO:0000269|PubMed:27545622}.
BINDING 386 386 AMP. {ECO:0000269|PubMed:27545622}.
SITE 74 74 Could play a key role in the
communication between the regulatory and
the substrate sites.
{ECO:0000305|PubMed:21741429}.
SITE 113 113 Could play a key role in the
communication between the regulatory and
the substrate sites.
{ECO:0000305|PubMed:21741429}.
VARIANT 44 44 A -> T (in SG14 mutant; lower apparent
affinities for substrates, fructose-1,6-
bisphosphate and AMP).
{ECO:0000269|PubMed:8385906}.
VARIANT 67 67 R -> C (in CL1136 mutant; less dependent
on the allosteric activator, fructose-
1,6-bisphosphate, for activity and less
sensitive to inhibition by AMP).
{ECO:0000269|PubMed:1339262}.
VARIANT 295 295 P -> S (in SG5 mutant).
{ECO:0000269|PubMed:1320612}.
VARIANT 336 336 G -> D (in 618 mutant; causes lowered
affinity for AMP).
{ECO:0000269|PubMed:2543670}.
MUTAGEN 39 39 K->E: The level of activation by
pyridoxal phosphate and fructose-1,6-
phosphate is only approximately 2-fold
compared to activation of 15- to 28-fold
respectively, for the wild-type. NADPH is
unable to activate the mutant enzyme.
{ECO:0000269|PubMed:2162151}.
MUTAGEN 74 74 Q->A: Insensitive to activation by
fructose-1,6-bisphosphate, but still
binds fructose-1,6-bisphosphate with
similar affinity as the wild-type. AMP
causes similar inhibition on the wild-
type and mutant.
{ECO:0000269|PubMed:21741429}.
MUTAGEN 74 74 Q->E: Insensitive to activation by
fructose-1,6-bisphosphate.
{ECO:0000269|PubMed:21741429}.
MUTAGEN 74 74 Q->N: The enzyme is activated 35-fold by
fructose-1,6-bisphosphate.
{ECO:0000269|PubMed:21741429}.
MUTAGEN 113 113 W->A: Insensitive to activation by
fructose-1,6-bisphosphate, but still
binds fructose-1,6-bisphosphate, with
similar affinity as the wild-type. AMP
causes similar inhibition on the wild-
type and mutant.
{ECO:0000269|PubMed:21741429}.
MUTAGEN 113 113 W->L: The enzyme is activated only 3-fold
by fructose-1,6-bisphosphate.
{ECO:0000269|PubMed:21741429}.
MUTAGEN 113 113 W->Y: The enzyme is activated 15-fold by
fructose-1,6-bisphosphate.
{ECO:0000269|PubMed:21741429}.
MUTAGEN 114 114 Y->F: Shows a decrease of affinity for
the substrates and less than 2-fold
activation by fructose 1,6-bisphosphate
in the ADP-glucose synthesis direction.
In contrast, in the pyrophosphorolysis
direction, the mutant shoqws about a 30-
fold activation by fructose 1,6-
bisphosphate.
{ECO:0000269|PubMed:2844780}.
MUTAGEN 195 195 K->E,I,H,R: Decrease of the affinity for
alpha-D-glucose 1-phosphate, but no loss
in adenylyltransferase activity.
{ECO:0000269|PubMed:1648099}.
MUTAGEN 195 195 K->Q: 600-fold decrease of the affinity
for alpha-D-glucose 1-phosphate compared
to the wild-type. In contrast, kinetic
constants for ATP, magnesium and
fructose-1,6-bisphosphate are similar in
mutant and wild-type cases. The catalytic
efficiency is 2-fold lower in the mutant.
{ECO:0000269|PubMed:1648099}.
CONFLICT 161 161 A -> V (in Ref. 3; CAA23544/AAA98736/
AAA23873). {ECO:0000305}.
CONFLICT 166 166 A -> V (in Ref. 3; CAA23544/AAA98736/
AAA23873). {ECO:0000305}.
CONFLICT 189 189 I -> T (in Ref. 3; CAA23544/AAA98736/
AAA23873). {ECO:0000305}.
CONFLICT 296 296 E -> K (in Ref. 3; CAA23544/AAA98736).
{ECO:0000305}.
HELIX 12 18 {ECO:0000244|PDB:5L6V}.
STRAND 20 25 {ECO:0000244|PDB:5L6V}.
HELIX 34 37 {ECO:0000244|PDB:5L6V}.
STRAND 38 40 {ECO:0000244|PDB:5L6V}.
HELIX 42 44 {ECO:0000244|PDB:5L6V}.
TURN 48 50 {ECO:0000244|PDB:5L6V}.
HELIX 54 63 {ECO:0000244|PDB:5L6V}.
STRAND 68 75 {ECO:0000244|PDB:5L6V}.
HELIX 78 87 {ECO:0000244|PDB:5L6V}.
HELIX 93 95 {ECO:0000244|PDB:5L6V}.
STRAND 98 103 {ECO:0000244|PDB:5L6V}.
STRAND 108 110 {ECO:0000244|PDB:5L6V}.
HELIX 117 123 {ECO:0000244|PDB:5L6V}.
HELIX 125 130 {ECO:0000244|PDB:5L6V}.
STRAND 134 140 {ECO:0000244|PDB:5L6V}.
HELIX 149 158 {ECO:0000244|PDB:5L6V}.
STRAND 162 171 {ECO:0000244|PDB:5L6V}.
HELIX 172 177 {ECO:0000244|PDB:5L6V}.
STRAND 178 183 {ECO:0000244|PDB:5L6V}.
STRAND 187 195 {ECO:0000244|PDB:5L6V}.
STRAND 208 219 {ECO:0000244|PDB:5L6V}.
HELIX 220 232 {ECO:0000244|PDB:5L6V}.
STRAND 233 235 {ECO:0000244|PDB:5L6S}.
TURN 240 243 {ECO:0000244|PDB:5L6V}.
HELIX 244 250 {ECO:0000244|PDB:5L6V}.
STRAND 254 258 {ECO:0000244|PDB:5L6V}.
HELIX 259 261 {ECO:0000244|PDB:5L6V}.
HELIX 280 289 {ECO:0000244|PDB:5L6V}.
STRAND 292 294 {ECO:0000244|PDB:5L6V}.
STRAND 316 319 {ECO:0000244|PDB:5L6V}.
STRAND 327 334 {ECO:0000244|PDB:5L6V}.
STRAND 339 342 {ECO:0000244|PDB:5L6V}.
STRAND 344 347 {ECO:0000244|PDB:5L6V}.
STRAND 361 367 {ECO:0000244|PDB:5L6V}.
STRAND 378 384 {ECO:0000244|PDB:5L6V}.
STRAND 395 398 {ECO:0000244|PDB:5L6V}.
HELIX 400 406 {ECO:0000244|PDB:5L6V}.
STRAND 407 409 {ECO:0000244|PDB:5L6V}.
STRAND 415 417 {ECO:0000244|PDB:5L6V}.
HELIX 419 424 {ECO:0000244|PDB:5L6V}.
SEQUENCE 431 AA; 48698 MW; 3C0A4C4F5B13D9D3 CRC64;
MVSLEKNDHL MLARQLPLKS VALILAGGRG TRLKDLTNKR AKPAVHFGGK FRIIDFALSN
CINSGIRRMG VITQYQSHTL VQHIQRGWSF FNEEMNEFVD LLPAQQRMKG ENWYRGTADA
VTQNLDIIRR YKAEYVVILA GDHIYKQDYS RMLIDHVEKG ARCTVACMPV PIEEASAFGV
MAVDENDKII EFVEKPANPP SMPNDPSKSL ASMGIYVFDA DYLYELLEED DRDENSSHDF
GKDLIPKITE AGLAYAHPFP LSCVQSDPDA EPYWRDVGTL EAYWKANLDL ASVVPELDMY
DRNWPIRTYN ESLPPAKFVQ DRSGSHGMTL NSLVSGGCVI SGSVVVQSVL FSRVRVNSFC
NIDSAVLLPE VWVGRSCRLR RCVIDRACVI PEGMVIGENA EEDARRFYRS EEGIVLVTRE
MLRKLGHKQE R


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DL-AMF-Ra Rat Glucose 6 Phosphate Isomerase (GPI) ELISA KitAMF,Autocrine motility factor,Glucose-6-phosphate isomerase,GPI,Gpi,Neuroleukin,NLK,PGI,PHI,Phosphoglucose isomerase,Phosphohexose isomerase 96T
E1185h ELISA kit Glucose transporter type 1, erythrocyte_brain,GLUT1,GLUT-1,HepG2 glucose transporter,Homo sapiens,Human,SLC2A1,Solute carrier family 2, facilitated glucose transporter member 1 96T
E1185h ELISA Glucose transporter type 1, erythrocyte_brain,GLUT1,GLUT-1,HepG2 glucose transporter,Homo sapiens,Human,SLC2A1,Solute carrier family 2, facilitated glucose transporter member 1 96T
U1185h CLIA Glucose transporter type 1, erythrocyte_brain,GLUT1,GLUT-1,HepG2 glucose transporter,Homo sapiens,Human,SLC2A1,Solute carrier family 2, facilitated glucose transporter member 1 96T
298-65701 Glucose Assay With the LabAssay Glucose Assay, when a sample is mixed with the Choromogen Reagent, the alpha_form of glucose in the sample is converted to beta_form by mutarotase. beta_DGlucose is oxi 1,000 tests
18-272-196361 Glucose Transporter GLUT1 - Rabbit polyclonal to Glucose Transporter GLUT1; Glucose transporter type 1. erythrocyte_brain; GLUT-1; HepG2 glucose transporter Polyclonal 0.5 ml
71662-16-3 glucose 1_(barium phosphate) glucose 1_(barium phos 1g
TM 324 TM 324 GLUCOSE PHOSPHATE BROTH (BUFFERED GLUCOSE BROTH) (MR_VP MEDIUM) (used in differentiation of bacteria by MR_VP test) 500 gm
TM 324 TM 324 GLUCOSE PHOSPHATE BROTH (BUFFERED GLUCOSE BROTH) (MR_VP MEDIUM) (used in differentiation of bacteria by MR_VP test) 100 gm
18-783-77669 RABBIT ANTI HUMAN GLUCOSE TRANSPORTER 5 (C-TERMINAL) - GLUT5; Glucose transporter type 8; GLUT-8; Glucose transporter type X1 Polyclonal 0.1 ml
18-272-196362 Glucose Transporter GLUT1 prediluted - Rabbit polyclonal to Glucose Transporter GLUT1 prediluted; Glucose transporter type 1. erythrocyte_brain; GLUT-1; HepG2 glucose transporter Polyclonal 7 ml


 

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