Entry |
|
Name |
arginine kinase;
arginine phosphokinase;
adenosine 5'-triphosphate: L-arginine phosphotransferase;
adenosine 5'-triphosphate-arginine phosphotransferase;
ATP:L-arginine N-phosphotransferasel ATP:L-arginine omega-N-phosphotransferase
|
Class |
Transferases;
Transferring phosphorus-containing groups;
Phosphotransferases with a nitrogenous group as acceptor
 |
Sysname |
ATP:L-arginine Nomega-phosphotransferase
|
Reaction(IUBMB) |
ATP + L-arginine = ADP + Nomega-phospho-L-arginine [RN: R00554]
|
Reaction(KEGG) |
|
Substrate |
|
Product |
ADP [CPD: C00008];
Nomega-phospho-L-arginine
|
History |
EC 2.7.3.3 created 1961
|
Pathway |
ec00330 | Arginine and proline metabolism |
|
Orthology |
|
Genes |
» show all
 |
Reference |
|
Authors |
ELODI P, SZORENYI E. |
Title |
Properties of crystalline arginine-phosphoferase isolated from Crustacean muscle. |
Journal |
Acta Physiol Hung 9:367-79 (1956) |
Reference |
|
Authors |
MORRISON JF, GRIFFITHS DE, ENNOR AH. |
Title |
The purification and properties of arginine phosphokinase. |
Journal |
Biochem J 65:143-53 (1957) |
Reference |
3 |
Authors |
Szorenyi, E.T., Dvornikova, P.D. and Degtyar, P.G. |
Title |
[Isolation in the crystalline state and some properties of adenosinetriphosphate-arginine transphosphorylase.]. |
Journal |
Dokl Akad Nauk SSSR 67:341-344 (1949) |
Reference |
|
Authors |
VIRDEN R, WATTS DC, BALDWIN E. |
Title |
ADENOSINE 5'-TRIPHOSPHATE-ARGININE PHOSPHOTRANSFERASE FROM LOBSTER MUSCLE: PURIFICATION AND PROPERTIES. |
Journal |
Biochem J 94:536-44 (1965) |
Other DBs |
ExplorEnz - The Enzyme Database: | 2.7.3.3 |
ExPASy - ENZYME nomenclature database: | 2.7.3.3 |
BRENDA, the Enzyme Database: | 2.7.3.3 |
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