BRENDA - Enzyme Database
show all sequences of 2.7.1.81

Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine

Veiga-da-Cunha, M.; Hadi, F.; Balligand, T.; Stroobant, V.; Van Schaftingen, E.; J. Biol. Chem. 287, 7246-7255 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0035
-
GTP
pH 7.1, 30C
Homo sapiens
0.0076
-
5-hydroxy-L-lysine
cosubstrate GTP, pH 7.1, 30C
Homo sapiens
0.28
-
5-hydroxy-L-lysine
cosubstrate ATP, pH 7.1, 30C
Homo sapiens
0.81
-
ATP
pH 7.1, 30C
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
A2RU49
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + 5-hydroxy-L-lysine
catalytic efficiency is 22fold higher with GTP than with ATP
720057
Homo sapiens
ADP + O-phosphohydroxy-L-lysine
-
-
-
?
GTP + 5-hydroxy-D-lysine
best substrate is the physiological form 5-hydroxy-L-lysine but human enzyme can also phosphorylate at a lower rate at least one other isomer
720057
Homo sapiens
GDP + O-phosphohydroxy-D-lysine
-
-
-
?
GTP + 5-hydroxy-L-lysine
best substrate is the physiological form 5-hydroxy-L-lysine but human enzyme can also phosphorylate at a lower rate at least one other isomer
720057
Homo sapiens
GDP + O-phosphohydroxy-L-lysine
-
-
-
?
additional information
no substrates for phosphorylation: ethanolamine, hydroxyproline, homoserine, serine, or choline
720057
Homo sapiens
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0035
-
GTP
pH 7.1, 30C
Homo sapiens
0.0076
-
5-hydroxy-L-lysine
cosubstrate GTP, pH 7.1, 30C
Homo sapiens
0.28
-
5-hydroxy-L-lysine
cosubstrate ATP, pH 7.1, 30C
Homo sapiens
0.81
-
ATP
pH 7.1, 30C
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + 5-hydroxy-L-lysine
catalytic efficiency is 22fold higher with GTP than with ATP
720057
Homo sapiens
ADP + O-phosphohydroxy-L-lysine
-
-
-
?
GTP + 5-hydroxy-D-lysine
best substrate is the physiological form 5-hydroxy-L-lysine but human enzyme can also phosphorylate at a lower rate at least one other isomer
720057
Homo sapiens
GDP + O-phosphohydroxy-D-lysine
-
-
-
?
GTP + 5-hydroxy-L-lysine
best substrate is the physiological form 5-hydroxy-L-lysine but human enzyme can also phosphorylate at a lower rate at least one other isomer
720057
Homo sapiens
GDP + O-phosphohydroxy-L-lysine
-
-
-
?
additional information
no substrates for phosphorylation: ethanolamine, hydroxyproline, homoserine, serine, or choline
720057
Homo sapiens
?
-
-
-
-
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
5
-
ATP
pH 7.1, 30C
Homo sapiens
12
-
5-hydroxy-L-lysine
cosubstrate ATP, pH 7.1, 30C
Homo sapiens
45
-
5-hydroxy-L-lysine
cosubstrate GTP, pH 7.1, 30C
Homo sapiens
110
-
GTP
pH 7.1, 30C
Homo sapiens
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
5
-
ATP
pH 7.1, 30C
Homo sapiens
12
-
5-hydroxy-L-lysine
cosubstrate ATP, pH 7.1, 30C
Homo sapiens
45
-
5-hydroxy-L-lysine
cosubstrate GTP, pH 7.1, 30C
Homo sapiens
110
-
GTP
pH 7.1, 30C
Homo sapiens
Other publictions for EC 2.7.1.81
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)
720057
Veiga-da-Cunha
Molecular identification of hy ...
Homo sapiens
J. Biol. Chem.
287
7246-7255
2012
-
-
1
-
-
-
-
4
-
-
-
-
-
2
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
4
4
642035
Chang
Guanosine triphosphate: 5-hydr ...
Rattus norvegicus
Enzyme
22
230-234
1977
-
-
-
-
-
-
7
1
-
1
-
1
-
1
-
-
1
-
-
1
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
1
-
1
-
1
-
-
-
1
-
1
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
642034
Hiles
The partial purification and p ...
Bos taurus, Cebus albifrons, Chlorocebus aethiops, Gallus gallus, Mus musculus, no activity in Homo sapiens, Oryctolagus cuniculus, Rattus norvegicus
J. Biol. Chem.
247
646-651
1972
-
-
-
-
-
-
16
2
-
8
-
1
-
9
-
-
1
-
-
12
1
1
3
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
16
-
2
-
8
-
1
-
-
-
1
-
12
1
1
3
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-