Information on EC 2.7.7.77 - molybdenum cofactor guanylyltransferase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.7.7.77
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RECOMMENDED NAME
GeneOntology No.
molybdenum cofactor guanylyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bis(guanylyl molybdenum cofactor) biosynthesis
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guanylyl molybdenum cofactor biosynthesis
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molybdenum cofactor biosynthesis
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Folate biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
GTP:molybdenum cofactor guanylyltransferase
Catalyses the guanylation of the molybdenum cofactor. This modification occurs only in prokaryotes.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + molybdenum cofactor
diphosphate + guanylyl molybdenum cofactor
show the reaction diagram
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-
?
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
show the reaction diagram
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0065 - 0.0706
GTP
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016 - 0.0053
GTP
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PDB 1FR9 and PDB 1FRW (complex with Mn-GTP)
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wild type PDB file 1E5K
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE cellulose column, Cibacron blue affinity column, Superose-12 gel filtration column
nickel-nitrilotriacetic acid column
using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D101A
inclusion bodies
D101N
reduced activity
G15L
inactive
G22L
wild type activity
G78L
wild type activity
G82L
reduced activity
K25A
reduced activity
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
wild type activity
N180D/N182D
wild type activity
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
R156A
reduced activity
R19A
wild type activity
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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Show AA Sequence (12878 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.7.77)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)