Enzyme(s) or Pathway(s)
No enzymes registered.
Possible Enzymes
Reported enzyme(s):
Possible enzyme(s):
1.14.18.2
CMP-N-acetylneuraminate monooxygenase
Reported enzyme(s):
Possible enzyme(s):
1.1.99.21
D-sorbitol dehydrogenase (acceptor)
2.3.1.21
carnitine O-palmitoyltransferase
2.3.1.28
chloramphenicol O-acetyltransferase
2.3.1.45
N-acetylneuraminate 7-O(or 9-O)-acetyltransferase
2.7.1.142
glycerol-3-phosphate-glucose phosphotransferase
2.7.1.26
riboflavin kinase
2.7.1.27
erythritol kinase
2.7.1.30
glycerol kinase
2.7.1.42
riboflavin phosphotransferase
2.7.1.79
diphosphate-glycerol phosphotransferase
3.1.1.23
acylglycerol lipase
3.1.1.34
lipoprotein lipase
3.1.1.5
lysophospholipase
3.1.1.60
bis(2-ethylhexyl)phthalate esterase
3.1.3.1
alkaline phosphatase
3.1.3.15
histidinol-phosphatase
3.1.3.2
acid phosphatase
3.1.3.21
glycerol-1-phosphatase
3.1.3.29
N-acylneuraminate-9-phosphatase
3.1.4.38
glycerophosphocholine cholinephosphodiesterase
3.1.4.43
glycerophosphoinositol inositolphosphodiesterase
3.2.1.22
alpha-galactosidase
3.2.1.23
beta-galactosidase
4.2.3.1
threonine synthase
Reported enzyme(s):
Possible enzyme(s):
2.4.1.167
sucrose 6F-alpha-galactotransferase
2.7.1.1
hexokinase
2.7.1.113
deoxyguanosine kinase
2.7.1.114
AMP-thymidine kinase
2.7.1.118
ADP-thymidine kinase
2.7.1.15
ribokinase
2.7.1.20
adenosine kinase
2.7.1.21
thymidine kinase
2.7.1.22
ribosylnicotinamide kinase
2.7.1.4
fructokinase
2.7.1.48
uridine kinase
2.7.1.56
1-phosphofructokinase
2.7.1.69
protein-N(pi)-phosphohistidine-sugar phosphotransferase
2.7.1.73
inosine kinase
2.7.1.74
deoxycytidine kinase
2.7.1.76
deoxyadenosine kinase
2.7.1.83
pseudouridine kinase
3.1.3.24
sucrose-phosphatase
3.1.3.35
thymidylate 5'-phosphatase
3.1.3.5
5'-nucleotidase
3.1.3.54
fructose-2,6-bisphosphate 6-phosphatase
3.1.3.68
2-deoxyglucose-6-phosphatase
3.1.3.73
alpha-ribazole phosphatase
3.1.5.1
dGTPase
Reported enzyme(s):
Possible enzyme(s):
2.7.1.23
NAD+ kinase
2.7.1.86
NADH kinase
3.1.3.6
3'-nucleotidase
Structure Data
Molfile
InChI
Simple COMPOUND page
Database Links
BiSSCat v1.06.20
http://bisscat.org/
Developed by Masaaki Kotera, Department of Biochemistry, Trinity College Dublin.
Science Foundation of Ireland is gratefully acknowledged.