BRENDA - Enzyme Database
show all sequences of 1.14.11.73

JMJD5 is a human arginyl C-3 hydroxylase

Wilkins, S.E.; Islam, M.S.; Gannon, J.M.; Markolovic, S.; Hopkinson, R.J.; Ge, W.; Schofield, C.J.; Chowdhury, R.; Nat. Commun. 9, 1180 (2018)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
structures of N-terminally truncated (aa 153-416 and aa 183-416) constructs and in complex with substrate RPS6. The JMJD5 active site contains a metal centre, which is octahedrally coordinated by an HXD..H motif, the 2-oxoglutarate oxalyl group and a water molecule, which is likely replaced by a dioxygen during catalysis
Homo sapiens
Engineering
Protein Variants
Commentary
Organism
H321A
substitution of Fe2+-binding residue, significantly reduces 2-oxoglutarate turnover
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
N-oxalylglycine
-
Homo sapiens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
-
Homo sapiens
Organism
Organism
UniProt
Commentary
Textmining
Homo sapiens
Q8N371
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
JMJD5 catalyses stereoselective C-3 hydroxylation of arginine residues in sequences from human regulator of chromosome condensation domain-containing protein 1 (RCCD1) and ribosomal protein S6 (RPS6)
757771
Homo sapiens
?
-
-
-
-
[RCCD1]-L-arginine + 2-oxoglutarate + O2
substrate i.e. regulator of chromosome condensation domain-containing protein 1
757771
Homo sapiens
[RCCD1]-(3R)-3-hydroxy-L-arginine + succinate + CO2
-
-
-
?
[RPS6]-L-arginine + 2-oxoglutarate + O2
substrate i.e. ribosomal protein S6
757771
Homo sapiens
[RPS6]-(3R)-3-hydroxy-L-arginine + succinate + CO2
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
JMJD5
-
Homo sapiens
KDM8
-
Homo sapiens
Crystallization (Commentary) (protein specific)
Crystallization
Organism
structures of N-terminally truncated (aa 153-416 and aa 183-416) constructs and in complex with substrate RPS6. The JMJD5 active site contains a metal centre, which is octahedrally coordinated by an HXD..H motif, the 2-oxoglutarate oxalyl group and a water molecule, which is likely replaced by a dioxygen during catalysis
Homo sapiens
Engineering (protein specific)
Protein Variants
Commentary
Organism
H321A
substitution of Fe2+-binding residue, significantly reduces 2-oxoglutarate turnover
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
N-oxalylglycine
-
Homo sapiens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
-
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
JMJD5 catalyses stereoselective C-3 hydroxylation of arginine residues in sequences from human regulator of chromosome condensation domain-containing protein 1 (RCCD1) and ribosomal protein S6 (RPS6)
757771
Homo sapiens
?
-
-
-
-
[RCCD1]-L-arginine + 2-oxoglutarate + O2
substrate i.e. regulator of chromosome condensation domain-containing protein 1
757771
Homo sapiens
[RCCD1]-(3R)-3-hydroxy-L-arginine + succinate + CO2
-
-
-
?
[RPS6]-L-arginine + 2-oxoglutarate + O2
substrate i.e. ribosomal protein S6
757771
Homo sapiens
[RPS6]-(3R)-3-hydroxy-L-arginine + succinate + CO2
-
-
-
?
Other publictions for EC 1.14.11.73
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
Synonyms
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)
757771
Wilkins
JMJD5 is a human arginyl C-3 ...
Homo sapiens
Nat. Commun.
9
1180
2018
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