2.7.3.4: taurocyamine kinase
This is an abbreviated version!
For detailed information about taurocyamine kinase, go to the full flat file.
Word Map on EC 2.7.3.4
-
2.7.3.4
-
creatine
-
glycocyamine
-
lombricine
-
annelid
-
polychaete
-
cdna-derived
-
arenicola
-
2.7.3.3
-
neanthes
-
paragonimus
-
phosphoarginine
-
westermani
-
drug development
-
pharmacology
- 2.7.3.4
- creatine
- glycocyamine
- lombricine
-
annelid
-
polychaete
-
cdna-derived
- arenicola
-
2.7.3.3
- neanthes
- paragonimus
- phosphoarginine
- westermani
- drug development
- pharmacology
Reaction
Synonyms
ATP:taurocyamine phosphotransferase, CsTK, guanidino kinase, hypotaurocyamine kinase, kinase (phosphorylating), taurocyamine, kinase, taurocyamine (phosphorylating), MiTK, More, phosphagen kinase, PK1, PK2, SmGK, taurocyamine kinase, taurocyamine phosphotransferase, TK, TPK
ECTree
Advanced search results
Subunits
Subunits on EC 2.7.3.4 - taurocyamine kinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
monomer
1 * 42000, SDS-PAGE, recombinant detagged D1 domain, SDS-PAGE, 1 * 80000, recombinant full-length enzyme, SDS-PAGE
additional information
2 + 51000, about, sequence calculation, the enzyme is dimeric but lacks cooperativity between the subunits in forming a transition state analogue complex
dimer
-
2 + 51000, about, sequence calculation, the enzyme is dimeric but lacks cooperativity between the subunits in forming a transition state analogue complex
-
-
SDS-PAGE reveals 3 protein bands: 11000 Da, 13000-14000 Da and 21000-22000 Da
additional information
the enzyme contains two domains, domain 1 and domain 2. The two domains function independently
additional information
-
the enzyme contains two domains, domain 1 and domain 2. The two domains function independently
additional information
the two unliganded lobes present a canonical open conformation and interact via their respective C- and N-terminal domains at a helix-mediated interface. The two lobes function independently
additional information
-
the two unliganded lobes present a canonical open conformation and interact via their respective C- and N-terminal domains at a helix-mediated interface. The two lobes function independently