KEGG   ENZYME: 2.7.3.3Help
Entry
EC 2.7.3.3                  Enzyme                                 

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
BRITE hierarchy
Sysname
ATP:L-arginine Nomega-phosphotransferase
Reaction(IUBMB)
ATP + L-arginine = ADP + Nomega-phospho-L-arginine [RN:R00554]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
L-arginine [CPD:C00062]
Product
ADP [CPD:C00008];
Nomega-phospho-L-arginine
History
EC 2.7.3.3 created 1961
Pathway
Arginine and proline metabolism
Orthology
K00934  
arginine kinase
Genes
DME: 
DPO: 
CEL: 
CELE_F44G3.2(F44G3.2) CELE_F46H5.3(F46H5.3) CELE_W10C8.5(W10C8.5) CELE_ZC434.8(ZC434.8)
TET: 
TBR: 
TCR: 
SUN: 
BCZ: 
BCZK0076(karG)
BCQ: 
BCQ_0094(karG)
BTK: 
BTL: 
BALH_0080(karG)
EAT: 
CTC: 
HOR: 
CTA: 
CTA_0733(karG)
MIN: 
 » show all
Taxonomy
Reference
1  [PMID:13339436]
  Authors
ELODI P, SZORENYI E.
  Title
Properties of crystalline arginine-phosphoferase isolated from Crustacean muscle.
  Journal
Acta. Physiol. Hung. 9 (1956) 367-79.
Reference
2  [PMID:13403885]
  Authors
MORRISON JF, GRIFFITHS DE, ENNOR AH.
  Title
The purification and properties of arginine phosphokinase.
  Journal
Biochem. J. 65 (1957) 143-53.
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 (1949) 341-344.
Reference
4  [PMID:14340045]
  Authors
VIRDEN R, WATTS DC, BALDWIN E.
  Title
ADENOSINE 5'-TRIPHOSPHATE-ARGININE PHOSPHOTRANSFERASE FROM LOBSTER MUSCLE: PURIFICATION AND PROPERTIES.
  Journal
Biochem. J. 94 (1965) 536-44.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9026-70-4

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