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Information on EC 2.7.7.77 - molybdenum cofactor guanylyltransferase and Organism(s) Escherichia coli and UniProt Accession P32173

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IUBMB Comments
Catalyses the guanylation of the molybdenum cofactor. This modification occurs only in prokaryotes.
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This record set is specific for:
Escherichia coli
UNIPROT: P32173
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
protein fa, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
nucleotidyl group transfer
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
GTP:molybdenum cofactor guanylyltransferase
Catalyses the guanylation of the molybdenum cofactor. This modification occurs only in prokaryotes.
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
-
-
-
?
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
show the reaction diagram
-
-
-
?
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
-
-
?
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0065 - 0.0706
GTP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016 - 0.0053
GTP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
molybdenum cofactor biosynthesis
metabolism
-
molybdenum cofactor biosynthesis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild type PDB file 1E5K
PDB 1FR9 and PDB 1FRW (complex with Mn-GTP)
-
PROTEIN VARIANTS
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-nitrilotriacetic acid column
using Ni-NTA chromatography
DEAE cellulose column, Cibacron blue affinity column, Superose-12 gel filtration column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team