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Information on EC 2.7.7.77 - molybdenum cofactor guanylyltransferase for references in articles please use BRENDA:EC2.7.7.77Word Map on EC 2.7.7.77
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The enzyme appears in viruses and cellular organisms
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molybdenum cofactor guanylyltransferase
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GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor
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nucleotidyl group transfer
nucleotidyl group transfer
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nucleotidyl group transfer
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bis(guanylyl molybdenum cofactor) biosynthesis
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guanylyl molybdenum cofactor biosynthesis
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molybdenum cofactor biosynthesis
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GTP:molybdenum cofactor guanylyltransferase
Catalyses the guanylation of the molybdenum cofactor. This modification occurs only in prokaryotes.
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MobA
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gene name
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UniProt
brenda
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SwissProt
brenda
K-12
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brenda
K-12
SwissProt
brenda
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metabolism
molybdenum cofactor biosynthesis
metabolism
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molybdenum cofactor biosynthesis
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GTP + molybdenum cofactor
diphosphate + guanylyl molybdenum cofactor
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GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
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GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
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GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
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GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
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GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
P32173
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GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
P95645
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0.0065
GTP
pH 7.2, temperature not specified in the publication, wild-type
0.0455
GTP
pH 7.2, temperature not specified in the publication, mutant L12T/G14A/P79L/A81T/G82S
0.0489
GTP
pH 7.2, temperature not specified in the publication, mutant L12T/G14A
0.0706
GTP
pH 7.2, temperature not specified in the publication, mutant P79L/A81T/G82S
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0.0016
GTP
pH 7.2, temperature not specified in the publication, mutant L12T/G14A/P79L/A81T/G82S
0.0041
GTP
pH 7.2, temperature not specified in the publication, mutant P79L/A81T/G82S
0.0048
GTP
pH 7.2, temperature not specified in the publication, wild-type
0.0053
GTP
pH 7.2, temperature not specified in the publication, mutant L12T/G14A
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Escherichia coli (strain K12);
P32173
Escherichia coli (strain K12);
P32173
Escherichia coli (strain K12);
P32173
Escherichia coli (strain K12);
P32173
Escherichia coli (strain K12);
P32173
Escherichia coli (strain K12);
P32173
Escherichia coli (strain K12);
P32173
Escherichia coli (strain K12);
P32173
Escherichia coli (strain K12);
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PDB 1FR9 and PDB 1FRW (complex with Mn-GTP)
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DEAE cellulose column, Cibacron blue affinity column, Superose-12 gel filtration column
nickel-nitrilotriacetic acid column
using Ni-NTA chromatography
DEAE cellulose column, Cibacron blue affinity column, Superose-12 gel filtration column
DEAE cellulose column, Cibacron blue affinity column, Superose-12 gel filtration column
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expressed in Escherichia coli as a His-tagged fusion protein
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L12T/G14A
Km (GTP) increased compared to wild-type, kcat slightly increased compared to wild-type, mutant shows 11-19 fold increased KD (GTP) dissociation constant compared to wild-type
L12T/G14A/P79L/A81T/G82S
Km (GTP) 7-10fold increased compared to wild-type, kcat 3fold decreased compared to wild-type,mutant shows 11-19 fold increased KD (GTP) dissociation constant compared to wild-type
N180D/N182D
wild type activity
P79L/A81T/G82S
Km (GTP) increased compared to wild-type, kcat slightly decreased compared to wild-type, mutant shows 11-19 fold increased KD (GTP) dissociation constant compared to wild-type
additional information
hybrid protein consisting of N-terminal MobA protein and C-terminal MocA protein shows similar Km (GTP) compared to wild-type, and increased kcat compared to wild-type, mutant shows comparable KD (GTP) dissociation constant compared to wild-type. Compared to wild-type Apo-TorA and TorD only interact with hybrid proteins that contain the C terminus of MobA, but no interaction is identified with variants containing the C terminus of MocA; hybrid protein consisting of N-terminal MocA protein and C-terminal MobA protein does not show any reactivity towards substrate GTP. Compared to wild-type Apo-TorA and TorD only interact with hybrid proteins that contain the C terminus of MobA, but no interaction is identified with variants containing the C terminus of MocA
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Temple, C.A.; Rajagopalan, K.V.
Mechanism of assembly of the Bis(Molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase
J. Biol. Chem.
275
40202-40210
2000
Rhodobacter sphaeroides (P95645)
brenda
Lake, M.W.; Temple, C.A.; Rajagopalan, K.V.; Schindelin, H.
The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis
J. Biol. Chem.
275
40211-40217
2000
Escherichia coli
brenda
Guse, A.; Stevenson, C.E.; Kuper, J.; Buchanan, G.; Schwarz, G.; Giordano, G.; Magalon, A.; Mendel, R.R.; Lawson, D.M.; Palmer, T.
Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA
J. Biol. Chem.
278
25302-25307
2003
Escherichia coli (P32173)
brenda
Neumann, M.; Seduk, F.; Iobbi-Nivol, C.; Leimkuhler, S.
Molybdopterin dinucleotide biosynthesis in Escherichia coli: Identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides
J. Biol. Chem.
286
1400-1408
2011
Escherichia coli (P32173)
brenda
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