Enzyme

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     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.57
Description:Diamine N-acetyltransferase.
Alternative Name: Spermidine N(1)-acetyltransferase.
Spermidine acetyltransferase.
Putrescine N-acetyltransferase.
Putrescine acetyltransferase.
Putrescine acetylase.
Putrescine (diamine)-acetylating enzyme.
Diamine acetyltransferase.
Acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase.
Cath: 1.10.287.90; 1.10.287.900; 3.40.630.30;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.57
BRENDA Enzyme Link: BRENDA 2.3.1.57
KEGG Enzyme Link: KEGG2.3.1.57
BioCyc Enzyme Link: BioCyc 2.3.1.57
ExPASy Enzyme Link: ExPASy2.3.1.57
EC2PDB Enzyme Link: EC2PDB 2.3.1.57
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.57
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.57
IntEnz Enzyme Link: IntEnz 2.3.1.57
MEDLINE Enzyme Link: MEDLINE 2.3.1.57
MSA:

2.3.1.57;

Phylogenetic Tree:

2.3.1.57;

Uniprot:
M-CSA:
RHEA:11116 acetyl-CoA + an alkane-alpha,omega-diamine = an N-acetylalkane-alpha,omega-diamine + CoA + H(+)
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Properties and structure of spermidine acetyltransferase in Escherichia coli.Fukuchi J, Kashiwagi K, Takio K, Igarashi K1994 Sep 98077207
Purification and characterization of spermidine/spermine N1-acetyltransferase from rat liver.Ragione FD, Pegg AE1982 Nov 237150547
Occurrence and induction of spermidine-N1-acetyltransferase in Escherichia coli.Matsui I, Kamei M, Otani S, Morisawa S, Pegg AE1982 Jun 307052085
The crystal structure of spermidine/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis.Montemayor EJ, Hoffman DW2008 Sep 218690703
Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase.Hegde SS, Chandler J, Vetting MW, Yu M, Blanchard JS2007 Jun 1917516632
Cryptosporidium parvum spermidine/spermine N1-acetyltransferase exhibits different characteristics from the host enzyme.Yarlett N, Wu G, Waters WR, Harp JA, Wannemuehler MJ, Morada M, Athanasopoulos D, Martinez MP, Upton SJ, Marton LJ, Frydman BJ2007 Apr17289169
Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target.Bewley MC, Graziano V, Jiang J, Matz E, Studier FW, Pegg AE, Coleman CS, Flanagan JM2006 Feb 1416455797
Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase.Forouhar F, Lee IS, Vujcic J, Vujcic S, Shen J, Vorobiev SM, Xiao R, Acton TB, Montelione GT, Porter CW, Tong L2005 Dec 216210326

RHEA:25181 acetyl-CoA + putrescine = CoA + H(+) + N-acetylputrescine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

RHEA:28150 acetyl-CoA + spermidine = CoA + H(+) + N(1)-acetylspermidine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Properties and structure of spermidine acetyltransferase in Escherichia coli.Fukuchi J, Kashiwagi K, Takio K, Igarashi K1994 Sep 98077207
Occurrence and induction of spermidine-N1-acetyltransferase in Escherichia coli.Matsui I, Kamei M, Otani S, Morisawa S, Pegg AE1982 Jun 307052085
The crystal structure of spermidine/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis.Montemayor EJ, Hoffman DW2008 Sep 218690703
Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase.Hegde SS, Chandler J, Vetting MW, Yu M, Blanchard JS2007 Jun 1917516632
Cryptosporidium parvum spermidine/spermine N1-acetyltransferase exhibits different characteristics from the host enzyme.Yarlett N, Wu G, Waters WR, Harp JA, Wannemuehler MJ, Morada M, Athanasopoulos D, Martinez MP, Upton SJ, Marton LJ, Frydman BJ2007 Apr17289169
Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target.Bewley MC, Graziano V, Jiang J, Matz E, Studier FW, Pegg AE, Coleman CS, Flanagan JM2006 Feb 1416455797
Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase.Forouhar F, Lee IS, Vujcic J, Vujcic S, Shen J, Vorobiev SM, Xiao R, Acton TB, Montelione GT, Porter CW, Tong L2005 Dec 216210326
Characterization of a novel spermidine/spermine acetyltransferase, BltD, from Bacillus subtilis.Woolridge DP, Martinez JD, Stringer DE, Gerner EW1999 Jun 1510359661

RHEA:28270 acetyl-CoA + spermidine = CoA + H(+) + N(8)-acetylspermidine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Properties and structure of spermidine acetyltransferase in Escherichia coli.Fukuchi J, Kashiwagi K, Takio K, Igarashi K1994 Sep 98077207
Characterization of a novel spermidine/spermine acetyltransferase, BltD, from Bacillus subtilis.Woolridge DP, Martinez JD, Stringer DE, Gerner EW1999 Jun 1510359661
P/CAF-mediated spermidine acetylation regulates histone acetyltransferase activity.Burgio G, Corona DF, Nicotra CM, Carruba G, Taibi G201627389534

RHEA:33099 acetyl-CoA + spermine = CoA + H(+) + N(1)-acetylspermine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The crystal structure of spermidine/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis.Montemayor EJ, Hoffman DW2008 Sep 218690703
Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase.Hegde SS, Chandler J, Vetting MW, Yu M, Blanchard JS2007 Jun 1917516632
Cryptosporidium parvum spermidine/spermine N1-acetyltransferase exhibits different characteristics from the host enzyme.Yarlett N, Wu G, Waters WR, Harp JA, Wannemuehler MJ, Morada M, Athanasopoulos D, Martinez MP, Upton SJ, Marton LJ, Frydman BJ2007 Apr17289169
Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target.Bewley MC, Graziano V, Jiang J, Matz E, Studier FW, Pegg AE, Coleman CS, Flanagan JM2006 Feb 1416455797
Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase.Forouhar F, Lee IS, Vujcic J, Vujcic S, Shen J, Vorobiev SM, Xiao R, Acton TB, Montelione GT, Porter CW, Tong L2005 Dec 216210326
Characterization of a novel spermidine/spermine acetyltransferase, BltD, from Bacillus subtilis.Woolridge DP, Martinez JD, Stringer DE, Gerner EW1999 Jun 1510359661