M00165
type: Enzyme
rlcp: p72
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/-.-.-.-
cath: Aminopeptidase
cath: Histone Acetyltransferase; Chain A
ec: https://purl.uniprot.org/enzyme/2.3.1.48
csa: 1cm0
uniprot: Q92830
uniprot: Q92831
kegg enzyme: histone acetyltransferase
kegg enzyme: nucleosome-histone acetyltransferase
kegg enzyme: histone acetokinase
kegg enzyme: histone acetylase
kegg enzyme: histone transacetylase
kegg substrate: Acetyl-CoA
kegg substrate: Histone
kegg product: CoA
kegg product: Acetylhistone
pdb: 1cm0A
pdb: 1cm0B
pdb: 1b91A
pdb: 1jm4B
pdb: 1f68A
pdb: 1n72A
pdb bound state: Unbound
  compound: Acetyl-CoA
  pdb: 1cm0A
pdb bound state: Unbound
  compound: Acetyl-CoA
  pdb: 1cm0B
pdb bound state: Unbound
  compound: Acetyl-CoA
  pdb: 1b91A
pdb bound state: Unbound
  compound: Acetyl-CoA
  pdb: 1jm4B
pdb bound state: Unbound
  compound: Acetyl-CoA
  pdb: 1f68A
pdb bound state: Unbound
  compound: Acetyl-CoA
  pdb: 1n72A
pdb bound state: Unbound
  compound: Histone
  pdb: 1cm0A
pdb bound state: Unbound
  compound: Histone
  pdb: 1cm0B
pdb bound state: Unbound
  compound: Histone
  pdb: 1b91A
pdb bound state: Unbound
  compound: Histone
  pdb: 1jm4B
pdb bound state: Unbound
  compound: Histone
  pdb: 1f68A
pdb bound state: Unbound
  compound: Histone
  pdb: 1n72A
pdb bound state: Unbound
  compound: CoA
  pdb: 1b91A
pdb bound state: Unbound
  compound: CoA
  pdb: 1jm4B
pdb bound state: Unbound
  compound: CoA
  pdb: 1f68A
pdb bound state: Unbound
  compound: CoA
  pdb: 1n72A
pdb bound state: Unbound
  compound: Acetylhistone
  pdb: 1cm0A
pdb bound state: Unbound
  compound: Acetylhistone
  pdb: 1cm0B
pdb bound state: Unbound
  compound: Acetylhistone
  pdb: 1b91A
pdb bound state: Unbound
  compound: Acetylhistone
  pdb: 1jm4B
pdb bound state: Unbound
  compound: Acetylhistone
  pdb: 1f68A
pdb bound state: Unbound
  compound: Acetylhistone
  pdb: 1n72A
active site residues resources: Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 2
  reference section: Fig.4C, p.3526-3528
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 3
  reference section: Fig.4, p.18160
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 14
  reference section: p.157-158
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 17
  reference section: Fig.3, p.438
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 20
  reference section: Fig.2E, p.556
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 21
  reference section: Fig.3A, p.115
references: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
references: Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A
references: Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
references: Structure and ligand of a histone acetyltransferase bromodomain
references: Structure and mechanism of action of the histone acetyltransferase Gcn5 and similarity to other N-acetyltransferases.
references: Kinetic mechanism of human histone acetyltransferase P/CAF
references: CREB-binding protein and p300
references: p300/CBP-associated factor histone acetyltransferase processing of a peptide substrate. Kinetic analysis of the catalytic mechanism
references: Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
references: Acetylation of histones and transcription-related factors.
references: The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc.
references: Matching the transcription machinery to the right DNA
references: Structure and function of histone acetyltransferases
references: Histone acetyltransferases
references: Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene
references: Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity
references: Structure of histone acetyltransferases.
references: Bromodomain: an acetyl-lysine binding domain.
references: Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain.
references: Insights into structure and function of GCN5/PCAF and yEsa 1 histone acetyltransferase domains:.
references: Biochemical and structural characterization of recombinant histone acetyltransferase proteins.
references: Use of nuclear magnetic resonance spectroscopy to study structure-function of bromodomains.
comment: According to the literature [2], the catalytic mechanism is similar to that of histone acetyltransferase type B (T00034 in EzCatDB). The reaction proceeds via a direct nucleophilic attack of the substrate histone lysine on the carbonyl carbon of acyl group of acetyl-CoA (see [2]). Hydrophobic residues (Phe563, Phe568, Ile571, Val572, Leu606, Ile637 & Tyr640) raise the pKa of the general base, Glu570. The mainchain amide of Cys574 stabilizes the tetrahedral intermediate.

Aminopeptidase
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.630.30
catalytic domain: index.html

Histone Acetyltransferase; Chain A
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.20.920.10

Acetyl-CoA
type: KeggSubstrate
references: KEGG:C00024
compound type: amine group
compound type: carbohydrate
compound type: nucleotide
compound type: peptide/protein
compound type: sulfide group
references: CHEBI:15351
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Histone
type: KeggSubstrate
references: KEGG:C01429
compound type: peptide/protein

CoA
type: KeggProduct
references: KEGG:C00010
compound type: amine group
compound type: carbohydrate
compound type: nucleotide
compound type: peptide/protein
compound type: sulfhydryl group
references: CHEBI:15346
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Acetylhistone
type: KeggProduct
references: KEGG:C01997
compound type: peptide/protein

1cm0A
type: Pdb
references: 1cm0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cm0
catalytic residue: GLU 570
main chain in catalysis: CYS 574

1cm0B
type: Pdb
references: 1cm0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cm0
catalytic residue: GLU 570
main chain in catalysis: CYS 574

A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8684459
journal: Nature
volume: 382
pages: 319-24
published year: 1996
authors:
  item: Yang XJ
  item: Ogryzko VV
  item: Nishikawa J
  item: Howard BH
  item: Nakatani Y

Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10393169
journal: EMBO J
volume: 18
pages: 3521-32
published year: 1999
authors:
  item: Clements A
  item: Rojas JR
  item: Trievel RC
  item: Wang L
  item: Berger SL
  item: Marmorstein R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10373413
journal: J Biol Chem
volume: 274
pages: 18157-60
published year: 1999
authors:
  item: Tanner KG
  item: Trievel RC
  item: Kuo MH
  item: Howard RM
  item: Berger SL
  item: Allis CD
  item: Marmorstein R
  item: Denu JM

Structure and ligand of a histone acetyltransferase bromodomain
type: BibliographicResource
comment: STRUCTURE BY NMR OF 715-832, AND MUTAGENESIS OF VAL-752; TYR-760; TYR-802 AND TYR-809.
medline id: 99292086
references: http://www.ncbi.nlm.nih.gov/pubmed/10365964
journal: Nature
volume: 399
pages: 491-6
published year: 1999
authors:
  item: Dhalluin C
  item: Carlson JE
  item: Zeng L
  item: He C
  item: Aggarwal AK
  item: Zhou MM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q92831

Structure and mechanism of action of the histone acetyltransferase Gcn5 and similarity to other N-acetyltransferases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10430845
journal: Proc Natl Acad Sci U S A
volume: 96
pages: 8807-8
published year: 1999
authors:
  item: Sternglanz R
  item: Schindelin H

Kinetic mechanism of human histone acetyltransferase P/CAF
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11009610
journal: Biochemistry
volume: 39
pages: 11961-9
published year: 2000
authors:
  item: Tanner KG
  item: Langer MR
  item: Denu JM

CREB-binding protein and p300
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10648382
journal: Blood
volume: 95
pages: 745-55
published year: 2000
authors:
  item: Blobel GA

p300/CBP-associated factor histone acetyltransferase processing of a peptide substrate. Kinetic analysis of the catalytic mechanism
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10777508
journal: J Biol Chem
volume: 275
pages: 21953-9
published year: 2000
authors:
  item: Lau OD
  item: Courtney AD
  item: Vassilev A
  item: Marzilli LA
  item: Cotter RJ
  item: Nakatani Y
  item: Cole PA

Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
type: BibliographicResource
comment: STRUCTURE BY NMR OF 730-832.
references: http://www.ncbi.nlm.nih.gov/pubmed/11090279
journal: J Mol Biol
volume: 304
pages: 355-70
published year: 2000
authors:
  item: Hudson BP
  item: Martinez-Yamout MA
  item: Dyson HJ
  item: Wright PE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q92830

Acetylation of histones and transcription-related factors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10839822
journal: Microbiol Mol Biol Rev
volume: 64
pages: 435-59
published year: 2000
authors:
  item: Sterner DE
  item: Berger SL

The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc.
type: BibliographicResource
comment: INTERACTION WITH TRRAP.
medline id: 10611234
references: http://www.ncbi.nlm.nih.gov/pubmed/10611234
journal: Mol Cell Biol
volume: 20
pages: 556-62
published year: 2000
authors:
  item: McMahon SB
  item: Wood MA
  item: Cole MD
references: Q92830

Matching the transcription machinery to the right DNA
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10847852
journal: Science
volume: 288
pages: 1372-3
published year: 2000
authors:
  item: Pennisi E

Structure and function of histone acetyltransferases
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11437231
journal: Cell Mol Life Sci
volume: 58
pages: 693-703
published year: 2001
authors:
  item: Marmorstein R

Histone acetyltransferases
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11250138
journal: Curr Opin Genet Dev
volume: 11
pages: 155-61
published year: 2001
authors:
  item: Marmorstein R
  item: Roth SY

Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11509556
journal: J Biol Chem
volume: 276
pages: 42753-60
published year: 2001
authors:
  item: Shankaranarayanan P
  item: Chaitidis P
  item: Kuhn H
  item: Nigam S

Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11445580
journal: J Biol Chem
volume: 276
pages: 33721-9
published year: 2001
authors:
  item: Thompson PR
  item: Kurooka H
  item: Nakatani Y
  item: Cole PA

Structure of histone acetyltransferases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11492997
journal: J Mol Biol
volume: 311
pages: 433-44
published year: 2001
authors:
  item: Marmorstein R

Bromodomain: an acetyl-lysine binding domain.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11911891
journal: FEBS Lett
volume: 513
pages: 124-8
published year: 2002
authors:
  item: Zeng L
  item: Zhou MM

Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain.
type: BibliographicResource
comment: NMR structure
references: http://www.ncbi.nlm.nih.gov/pubmed/11931765
journal: Mol Cell
volume: 9
pages: 575-86
published year: 2002
authors:
  item: Mujtaba S
  item: He Y
  item: Zeng L
  item: Farooq A
  item: Carlson JE
  item: Ott M
  item: Verdin E
  item: Zhou MM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Insights into structure and function of GCN5/PCAF and yEsa 1 histone acetyltransferase domains:.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14712728
journal: Methods Enzymol
volume: 371
pages: 545-64
published year: 2003
authors:
  item: Clements A
  item: Marmorstein R

Biochemical and structural characterization of recombinant histone acetyltransferase proteins.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14975301
journal: Methods Enzymol
volume: 376
pages: 106-19
published year: 2004
authors:
  item: Marmorstein R

Use of nuclear magnetic resonance spectroscopy to study structure-function of bromodomains.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14975302
journal: Methods Enzymol
volume: 376
pages: 119-30
published year: 2004
authors:
  item: Mujtaba S
  item: Zhou MM