Sequence of APAH_MYCRA
EC Number:3.5.1.62
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
N-acetylputrescine + H2O = acetate + putrescine
Other sequences found for EC No. 3.5.1.62
General information:
Sequence
0 MRVIFSEDHK LRNAKTELYG GELVPPFEAP FRAEWILAAV KEAGFDDVVA PARHGLETVL
60 KVHDAGYLNF LETAWDRWKA AGYKGEAIAT SFPVRRTSPR IPTDIEGQIG YYCNAAETAI
120 SPGTWEAALS SMASAIDGAD LIAAGHKAAF SLCRPPGHHA GIDMFGGYCF INNAAVAAQR
180 LLDKGAKKIA ILDVDFHHGN GTQDIFYERG DVFFASLHGD PAEAFPHFLG YAEETGKGAG
240 AGTTANYPMG RGTPYSVWGE ALTDSLKRIA AFGAEAIVVS LGVDTFEQDP ISFFKLTSPD
300 YITMGRTIAA SGVPLLVVME GGYGVPEIGL NVANVLKGVA G
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1157105
Sakurada K.,Ohta T.,Fujishiro K.,Hasegawa M.,Aisaka K.
Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme.
J. Bacteriol.
178
5781-5786
1996
1157106
Fujishiro K.,Ando M.,Uwajima T.
Crystallization and some properties of acetylpolyamine amidohydrolase from Mycoplana bullata.
Biochem. Biophys. Res. Commun.
157
1169-1174
1988
1157107
Lombardi P.M.,Angell H.D.,Whittington D.A.,Flynn E.F.,Rajashankar K.R.,Christianson D.W.
Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases.
Biochemistry
50
1808-1817
2011
1157108
Decroos C.,Christianson D.W.
Design, synthesis, and evaluation of polyamine deacetylase inhibitors, and high-resolution crystal structures of their complexes with acetylpolyamine amidohydrolase.
Biochemistry
54
4692-4703
2015
