Information on EC 3.1.4.49 - dolichylphosphate-mannose phosphodiesterase

for references in articles please use BRENDA:EC3.1.4.49
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.4.49
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RECOMMENDED NAME
GeneOntology No.
dolichylphosphate-mannose phosphodiesterase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dolichyl beta-D-mannosyl phosphate + H2O = dolichyl phosphate + D-mannose
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric diester
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SYSTEMATIC NAME
IUBMB Comments
dolichyl-beta-D-mannosyl-phosphate dolichylphosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
111839-07-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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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
mannosylphosphodolichol + H2O
D-mannose + dolichyl phosphate
show the reaction diagram
additional information
?
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not: N-acetylglucosaminyldiphosphodolichol, glucosylphosphodolichol or mannose 1-phosphate, artificial substrates for acid phosphatase, acid phosphodiesterase, mannosidase or glucosidase
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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
mannosylphosphodolichol + H2O
D-mannose + dolichyl phosphate
show the reaction diagram
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enzyme may be capable of degrading Dol-P-Man in vivo
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
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greatly stimulates, optimum concentration: 2 mM
additional information
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not activated by other divalent cations than Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bis(4-nitrophenyl)phosphate
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1 mM, competitive inhibition
dolichol
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0.1 mM, strong, competitive inhibition
dolichyl phosphate
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0.1 mM, strong, competitive inhibition
additional information
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not inhibited by D-mannose, mannose 1-phosphate, GDP, GMP, ADP, AMP, phosphate, diphosphate GDPmannose, UDP-N-acetylglucosamine, UDPglucose, UDPglucuronic acid, 4-nitrophenyl phosphate, 4-nitrophenyl-alpha-D-mannopyranoside, 4-nitrophenyl-beta-D-mannopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside or 4-nitrophenyl-beta-D-glucopyranoside
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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requirement, or other SH-reducing agents
Emulgen 909
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requirement, optimum concentration: 0.4% v/v
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SH-reducing agents
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e.g. 2-mercaptoethanol, absolute requirement
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additional information
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no requirement for any phospholipid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00043
Mannosylphosphodolichol
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pH 5.3, 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0125
dolichyl phosphate
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pH 5.3, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000011
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pH 6.3
0.000631
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pH 5.3, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
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acetate buffer
6.3
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
a heat-stable factor, precipitable by trichloroacetic acid, insoluble in lipid solvents, stabilizes, separation from this factor by ion-exchange chromatography inactivates irreversibly
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, in the presence of 2-mercaptoethanol and stabilizing factor, 1 month, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial, 57.9fold, solubilized with 1% v/v Emulgen 909
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