EC number:2.3.1.257
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.3 Acyltransferases |
| 2.3.1 Transferring groups other than aminoacyl groups |
| ID: | 2.3.1.257 |
|---|---|
| Description: | N-terminal L-serine N(alpha)-acetyltransferase NatD. |
| Cath: | 3.40.630.30; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.3.1.257 |
| BRENDA Enzyme Link: | BRENDA 2.3.1.257 |
| KEGG Enzyme Link: | KEGG2.3.1.257 |
| BioCyc Enzyme Link: | BioCyc 2.3.1.257 |
| ExPASy Enzyme Link: | ExPASy2.3.1.257 |
| EC2PDB Enzyme Link: | EC2PDB 2.3.1.257 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.3.1.257 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.3.1.257 |
| IntEnz Enzyme Link: | IntEnz 2.3.1.257 |
| MEDLINE Enzyme Link: | MEDLINE 2.3.1.257 |
EC number:2.3.1.257
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:50600 | acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A] |
| 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
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD. | Magin RS, Liszczak GP, Marmorstein R | 2015 Feb 3 | 25619998 |
| The human N-alpha-acetyltransferase 40 (hNaa40p/hNatD) is conserved from yeast and N-terminally acetylates histones H2A and H4. | Hole K, Van Damme P, Dalva M, Aksnes H, Glomnes N, Varhaug JE, Lillehaug JR, Gevaert K, Arnesen T | 2011 | 21935442 |
| Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4. | Polevoda B, Hoskins J, Sherman F | 2009 Jun | 19332560 |
| An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. | Song OK, Wang X, Waterborg JH, Sternglanz R | 2003 Oct 3 | 12915400 |
| RHEA:50596 | acetyl-CoA + N-terminal L-seryl-[histone H4] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H4] |
| 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
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD. | Magin RS, Liszczak GP, Marmorstein R | 2015 Feb 3 | 25619998 |
| The human N-alpha-acetyltransferase 40 (hNaa40p/hNatD) is conserved from yeast and N-terminally acetylates histones H2A and H4. | Hole K, Van Damme P, Dalva M, Aksnes H, Glomnes N, Varhaug JE, Lillehaug JR, Gevaert K, Arnesen T | 2011 | 21935442 |
| Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4. | Polevoda B, Hoskins J, Sherman F | 2009 Jun | 19332560 |
| An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. | Song OK, Wang X, Waterborg JH, Sternglanz R | 2003 Oct 3 | 12915400 |