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
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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
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)