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FGROUP
SUBSTRUCTURE
compound
enzyme
Multiple
N-Acetylputrescine
Enzyme(s) or Pathway(s)
3.5.1.62
acetylputrescine deacetylase
Possible Enzymes
Reported enzyme(s):
1.4.3.4
amine oxidase (flavin-containing)
Possible enzyme(s):
Reported enzyme(s):
2.3.1.57
diamine N-acetyltransferase
3.5.1.51
4-acetamidobutyryl-CoA deacetylase
3.5.1.62
acetylputrescine deacetylase
Possible enzyme(s):
Reported enzyme(s):
Possible enzyme(s):
1.14.18.2
CMP-N-acetylneuraminate monooxygenase
Reported enzyme(s):
Possible enzyme(s):
1.5.3.11
polyamine oxidase
1.5.99.6
spermidine dehydrogenase
2.1.1.103
phosphoethanolamine N-methyltransferase
2.1.1.53
putrescine N-methyltransferase
2.1.3.3
ornithine carbamoyltransferase
2.1.3.6
putrescine carbamoyltransferase
2.1.4.1
glycine amidinotransferase
2.1.4.2
scyllo-inosamine-4-phosphate amidinotransferase
2.3.1.127
ornithine N-benzoyltransferase
2.3.1.138
putrescine N-hydroxycinnamoyltransferase
2.3.1.64
agmatine N4-coumaroyltransferase
2.5.1.16
spermidine synthase
2.5.1.22
spermine synthase
2.5.1.23
sym-norspermidine synthase
2.5.1.44
homospermidine synthase
2.5.1.45
homospermidine synthase (spermidine-specific)
2.5.1.46
deoxyhypusine synthase
2.6.1.11
acetylornithine transaminase
2.6.1.13
ornithine-oxo-acid transaminase
2.6.1.29
diamine transaminase
2.6.1.46
diaminobutyrate-pyruvate transaminase
2.6.1.48
5-aminovalerate transaminase
2.7.3.10
agmatine kinase
3.5.1.20
citrullinase
3.5.1.40
acylagmatine amidase
3.5.1.53
N-carbamoylputrescine amidase
3.5.1.60
N-(long-chain-acyl)ethanolamine deacylase
3.5.1.63
4-acetamidobutyrate deacetylase
3.5.3.1
arginase
3.5.3.10
D-arginase
3.5.3.11
agmatinase
3.5.3.20
diguanidinobutanase
3.5.3.22
proclavaminate amidinohydrolase
3.5.3.7
guanidinobutyrase
6.3.1.9
trypanothione synthase
Reported enzyme(s):
Possible enzyme(s):
2.3.1.59
gentamicin 2'-N-acetyltransferase
2.3.1.87
aralkylamine N-acetyltransferase
3.5.1.17
acyl-lysine deacylase
3.5.1.21
N-acetyl-beta-alanine deacetylase
Structure Data
Molfile
InChI
Simple COMPOUND page
Database Links
PubChem:5677
KEGG:C02714
ChEBI:17768
BiSSCat v1.06.20
http://bisscat.org/
Developed by Masaaki Kotera, Department of Biochemistry, Trinity College Dublin.
Science Foundation of Ireland is gratefully acknowledged.