Information on EC 3.6.1.42 - guanosine-diphosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.1.42
-
RECOMMENDED NAME
GeneOntology No.
guanosine-diphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GDP + H2O = GMP + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of diphosphate bonds
-
-
-
-
hydrolysis of phosphoric ester
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NIL
-
-
SYSTEMATIC NAME
IUBMB Comments
GDP phosphohydrolase
Also acts on UDP but not on other nucleoside diphosphates and triphosphates.
CAS REGISTRY NUMBER
COMMENTARY hide
98037-56-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
calf
-
-
Manually annotated by BRENDA team
gene gda1
SwissProt
Manually annotated by BRENDA team
enzyme KlGdap1
SwissProt
Manually annotated by BRENDA team
Syrian hamster, normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity
-
-
Manually annotated by BRENDA team
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + H2O
AMP + phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
-
low activity
-
-
?
GDP + H2O
5'-GMP + phosphate
show the reaction diagram
GDP + H2O
GMP + phosphate
show the reaction diagram
IDP + H2O
IMP + phosphate
show the reaction diagram
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
show the reaction diagram
-
reaction of EC 3.6.1.17
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
additional information
?
-
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
GDP + H2O
5'-GMP + phosphate
show the reaction diagram
GDP + H2O
GMP + phosphate
show the reaction diagram
UDP + H2O
UMP + phosphate
show the reaction diagram
Q9HEM6
the enzyme's UDPase activity plays a role in uridine nucleotide sugar transport into Golgi vesicles
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Divalent cations
-
required
Fe2+
-
less than 10% activation
Ni2+
-
less than 10% activation
Zn2+
-
less than 10% activation
additional information
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP
-
hydrolysis of UDP
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,4,5,6-pentaphosphate
competitive
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
competitive
inositol 4-butyl-1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
competitive
UDP
-
hydrolysis of GDP
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triton X-100
-
0.1% Triton X-100: 6-10fold activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3830
GDP
Saccharomyces cerevisiae
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00011
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,4,5,6-pentaphosphate
pH not specified in the publication, temperature not specified in the publication
0.00027
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
pH not specified in the publication, temperature not specified in the publication
0.000023
inositol 4-butyl-1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4000
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 8.2
-
broad pH optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
-
calf, gel filtration and glycerol density gradient centrifugation
47000
-
deglycosylated GDPase, result of proteolytic cleavage of the 55000 Da enzyme during purification, SDS-PAGE
48000
-
deglycosylated GDPase, result of proteolytic cleavage of the 57000 Da enzyme during purification, SDS-PAGE
56820
-
calculated from amino acid sequence
57000
-
before signal sequence cleavage, metabolic labeling and immunoprecipitation, SDS-PAGE
120000
-
functional target size, irradiation of membranes from wild-type and gda1 null mutants
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 46000, calf, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to several cycles of freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, separated into aliquots, stable for a long time
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity, recombinant proteins from Escherichia coli BL21, DE3. Purified bacterial recombinant PCPH and mt-PCPH proteins have GDPase activity
-
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, functional complementation of a Saccharomyces GDPase null mutant
DNA sequence determination and analysis, enzyme can complement and restore activity in Saccharomyces cerevisiae deletion mutant gda1, complementation of N-glycosylation defects
GDA1 gene; overexpression of GDA1 gene
-
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity, expression in Escherichia coli BL21, DE3
-
overexpression in Schizosaccharomyces pombe, functional complementation of a Saccharomyces cerevisiae enzyme mutant defective in chitinase O-mannosylation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information