Literature summary for 2.7.3.2 extracted from

Wang, S.; Wang, X.; Shi, W.; Wang, K.; Ma, H.
Detection of local polarity and conformational changes at the active site of rabbit muscle creatine kinase with a new arginine-specific fluorescent probe (2008), Biochim. Biophys. Acta, 1784, 415-422.

Search for more literature for 2.7.3.2

General Stability

General Stability	Organism
the activity of the 3-(4-chloro-6-p-glyoxal-phenoxy-1,3,5-triazinylamino)-7-(dimethylamino)-2-methylphenazine-labeled creatine kinase is found to be about 40% of that of the native creatine kinase, which supports that the modified arginine residue by 3-(4-chloro-6-p-glyoxal-phenoxy-1,3,5-triazinylamino)-7-(dimethylamino)-2-methylphenazine is at the active site	Oryctolagus cuniculus

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	-	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + creatine	-	Oryctolagus cuniculus	ADP + creatine phosphate	-	?

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Oryctolagus cuniculus

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Release 2023.1 (January 2023)