BRENDA - Enzyme Database
show all sequences of 3.1.3.51

A dolichyl phosphate-cleaving acid phosphatase from Tetrahymena pyriformis

Adrian, G.S.; Keenan, R.W.; Biochim. Biophys. Acta 575, 431-438 (1979)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Ethoxy formic anhydride
10 mM, 67% inhibition of dolichyl phosphate hydrolysis, no inhibition of p-nitrophenyl phosphate cleavage
Tetrahymena pyriformis
Tartrate
inhibits hydrolysis of p-nitrophenyl phosphate, no inhibition of the hydrolysis of dolichyl phosphate
Tetrahymena pyriformis
vanadium oxide
inhibits hydrolysis of p-nitrophenyl phosphate and dolichyl phosphate
Tetrahymena pyriformis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
hydrolysis of dolichyl phosphate requires Mg2+
Tetrahymena pyriformis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Tetrahymena pyriformis
the enzyme is required for the regulation of the level of dolichyl phosphate and thus the rate of glycoprotein synthesis
?
-
-
-
additional information
Tetrahymena pyriformis WH14
the enzyme is required for the regulation of the level of dolichyl phosphate and thus the rate of glycoprotein synthesis
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Tetrahymena pyriformis
-
-
-
Tetrahymena pyriformis WH14
-
-
-
Storage Stability
Storage Stability
Organism
-20C, stable for several months
Tetrahymena pyriformis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dolichyl phosphate + H2O
-
134907
Tetrahymena pyriformis
dolichol + phosphate
-
-
-
?
dolichyl phosphate + H2O
-
134907
Tetrahymena pyriformis WH14
dolichol + phosphate
-
-
-
?
additional information
the enzyme is required for the regulation of the level of dolichyl phosphate and thus the rate of glycoprotein synthesis
134907
Tetrahymena pyriformis
?
-
-
-
-
additional information
the enzyme is required for the regulation of the level of dolichyl phosphate and thus the rate of glycoprotein synthesis
134907
Tetrahymena pyriformis WH14
?
-
-
-
-
p-nitrophenyl phosphate + H2O
-
134907
Tetrahymena pyriformis
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
-
134907
Tetrahymena pyriformis WH14
p-nitrophenol + phosphate
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
40
-
reaction rate increases up to
Tetrahymena pyriformis
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
50
-
10 min, 75% loss of activity
Tetrahymena pyriformis
60
-
10 min, complete loss of activity
Tetrahymena pyriformis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
6
-
Tetrahymena pyriformis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ethoxy formic anhydride
10 mM, 67% inhibition of dolichyl phosphate hydrolysis, no inhibition of p-nitrophenyl phosphate cleavage
Tetrahymena pyriformis
Tartrate
inhibits hydrolysis of p-nitrophenyl phosphate, no inhibition of the hydrolysis of dolichyl phosphate
Tetrahymena pyriformis
vanadium oxide
inhibits hydrolysis of p-nitrophenyl phosphate and dolichyl phosphate
Tetrahymena pyriformis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
hydrolysis of dolichyl phosphate requires Mg2+
Tetrahymena pyriformis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Tetrahymena pyriformis
the enzyme is required for the regulation of the level of dolichyl phosphate and thus the rate of glycoprotein synthesis
?
-
-
-
additional information
Tetrahymena pyriformis WH14
the enzyme is required for the regulation of the level of dolichyl phosphate and thus the rate of glycoprotein synthesis
?
-
-
-
Storage Stability (protein specific)
Storage Stability
Organism
-20C, stable for several months
Tetrahymena pyriformis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dolichyl phosphate + H2O
-
134907
Tetrahymena pyriformis
dolichol + phosphate
-
-
-
?
dolichyl phosphate + H2O
-
134907
Tetrahymena pyriformis WH14
dolichol + phosphate
-
-
-
?
additional information
the enzyme is required for the regulation of the level of dolichyl phosphate and thus the rate of glycoprotein synthesis
134907
Tetrahymena pyriformis
?
-
-
-
-
additional information
the enzyme is required for the regulation of the level of dolichyl phosphate and thus the rate of glycoprotein synthesis
134907
Tetrahymena pyriformis WH14
?
-
-
-
-
p-nitrophenyl phosphate + H2O
-
134907
Tetrahymena pyriformis
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
-
134907
Tetrahymena pyriformis WH14
p-nitrophenol + phosphate
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
40
-
reaction rate increases up to
Tetrahymena pyriformis
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
50
-
10 min, 75% loss of activity
Tetrahymena pyriformis
60
-
10 min, complete loss of activity
Tetrahymena pyriformis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
6
-
Tetrahymena pyriformis
Other publictions for EC 3.1.3.51
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
134922
Frank
Purification and characterizat ...
Bos taurus, Sus scrofa
J. Biol. Chem.
273
11791-11798
1998
-
-
-
-
-
-
10
2
2
1
1
-
-
4
-
-
1
-
-
3
1
-
4
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
10
-
2
2
1
1
-
-
-
-
1
-
3
1
-
4
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
134921
Bhat
Developmental changes in enzym ...
Rattus norvegicus
J. Neurochem.
56
339-344
1991
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
134913
Sumbilla
Dolichol kinase, phosphatase, ...
Bos taurus
Methods Enzymol.
111
471-482
1988
1
-
-
-
-
-
4
1
2
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
4
-
1
2
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
134906
Ravi
-
Submicrosomal distribution of ...
Glycine max
Biochim. Biophys. Acta
884
497-501
1986
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
134911
Keller
Characterization of polyisopre ...
Rattus norvegicus
Arch. Biochem. Biophys.
249
207-214
1986
-
-
-
-
-
-
6
-
1
-
-
-
-
2
-
-
-
-
-
2
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
-
-
2
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
134912
Scher
Dolichyl phosphate metabolism ...
Sus scrofa
J. Biol. Chem.
260
13742-13746
1985
-
-
-
-
-
-
-
2
1
-
-
-
-
3
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
134915
Boscoboinik
Dolichyl phosphate phosphatase ...
Rattus norvegicus
Biochim. Biophys. Acta
794
41-48
1984
9
-
-
-
-
-
4
-
2
-
1
-
-
2
-
-
-
-
-
2
-
1
1
-
2
-
-
-
-
-
-
-
1
-
-
9
-
-
-
-
-
-
-
4
1
-
2
-
1
-
-
-
-
-
-
2
-
1
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
134916
Rip
The submicrosomal distribution ...
Rattus norvegicus
J. Biol. Chem.
258
14926-14930
1983
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
134920
Ravi
Characterization of dolichol a ...
Glycine max
Biochem. J.
213
513-518
1983
3
-
-
-
-
-
4
1
1
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
3
-
-
-
-
-
-
-
4
-
1
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
134917
Belocopitow
Dolichyl-phosphate phosphatase ...
Rattus norvegicus
Eur. J. Biochem.
125
167-173
1982
-
-
-
-
-
-
8
1
1
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
1
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
134918
Rupar
The subcellular localization o ...
Rattus norvegicus
J. Biol. Chem.
257
3090-3094
1982
-
-
-
-
-
-
-
-
4
-
-
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
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-
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-
-
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-
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4
-
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-
-
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-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
134910
Rip
Localization of a dolichyl pho ...
Rattus norvegicus
J. Biol. Chem.
256
1929-1934
1981
-
-
-
-
-
-
5
1
2
1
-
-
-
2
-
-
-
-
-
3
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
1
2
1
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
134914
Burton
Enzymatic dephosphorylation of ...
Bos taurus
Arch. Biochem. Biophys.
208
409-417
1981
-
-
-
-
-
-
5
1
1
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
1
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
134919
Adrian
Dolichyl phosphate phosphatase ...
Tetrahymena pyriformis
Biochem. J.
197
233-238
1981
-
-
-
-
-
-
6
-
3
1
2
-
-
3
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
3
1
2
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
134908
Wedgwood
Enzymatic activities in cultur ...
Homo sapiens
J. Biol. Chem.
255
1120-1123
1980
-
-
-
-
-
-
1
1
1
-
-
-
-
2
-
-
-
-
-
1
1
-
1
-
-
-
-
-
1
1
-
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-
-
-
-
-
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
134909
Idoyaga-Vargas
A phosphatase acting on dolich ...
Rattus norvegicus
FEBS Lett.
112
63-66
1980
1
-
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-
-
-
-
-
2
-
-
1
-
1
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-
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-
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-
2
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1
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2
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1
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-
-
2
-
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-
-
-
-
-
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-
-
-
-
-
-
-
134907
Adrian
A dolichyl phosphate-cleaving ...
Tetrahymena pyriformis, Tetrahymena pyriformis WH14
Biochim. Biophys. Acta
575
431-438
1979
-
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-
-
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3
-
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1
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2
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3
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1
6
-
1
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2
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1
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3
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1
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2
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1
6
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1
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2
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1
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