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Information on EC 2.3.1.36 - D-amino-acid N-acetyltransferase
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2.3.1.36 D-amino-acid N-acetyltransferaseSpecify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
acetyltransferase, D-amino acid, D-amino acid acetyltransferase, D-amino acid-alpha-N-acetyltransferase, DNT, Hpa3p, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyltransferase, D-amino acid
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-
-
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D-amino acid acetyltransferase
D-amino acid-alpha-N-acetyltransferase
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-
-
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D-amino acid acetyltransferase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + a D-amino acid = CoA + an N-acetyl-D-amino acid
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-
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acetyl-CoA + a D-amino acid = CoA + an N-acetyl-D-amino acid
ordered bi bi mechanism with acetyl-CoA being the first substrate to be bound and CoA the last product to be released, involving acetylation of Cys304
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:D-amino-acid N-acetyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
37257-15-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + D-alpha-aminobutyrate
CoA + N-acetyl-D-alpha-aminobutyrate
-
-
-
-
?
acetyl-CoA + D-asparaginate
CoA + N-acetyl-D-asparaginate
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-
-
-
ir
propionyl-CoA + D-allo-isoleucine
CoA + N-propionyl-D-allo-isoleucine
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-
-
-
ir
propionyl-CoA + D-glutamine
CoA + N-propionyl-D-glutamine
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-
-
-
ir
propionyl-CoA + D-tryptophan
CoA + N2-propionyl-D-tryptophan
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-
-
ir
acetyl-CoA + a D-amino acid
CoA + an N-acetyl-D-amino acid
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-
-
-
?
acetyl-CoA + a D-amino acid
CoA + an N-acetyl-D-amino acid
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substrate specificity, overview
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-
?
acetyl-CoA + a D-amino acid
CoA + an N-acetyl-D-amino acid
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D-amino acids are toxic to Saccharomyces cerevisiae but are detoxified with D-amino acid-N-acetyltransferase by N-acetylation preceding removal from yeast cells
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-
?
acetyl-CoA + D-phenylalanine
CoA + N-acetyl-D-phenylalanine
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-
-
-
?
acetyl-CoA + D-phenylalanine
CoA + N-acetyl-D-phenylalanine
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-
-
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ir
acetyl-CoA + D-tryptophan
CoA + N-acetyl-D-tryptophan
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-
-
-
?
acetyl-CoA + D-tryptophan
CoA + N-acetyl-D-tryptophan
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-
-
ir
additional information
?
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L-isomers are not accepted, glycine and D-taurine are poor substrates, propionyl-CoA can replace acetyl-CoA
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?
additional information
?
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no activity with L-lysine, D-proline, and D-aspartate, D-glutamate is a poor substrate
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + D-asparaginate
CoA + N-acetyl-D-asparaginate
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-
-
-
ir
acetyl-CoA + D-phenylalanine
CoA + N-acetyl-D-phenylalanine
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-
-
-
ir
acetyl-CoA + D-tryptophan
CoA + N-acetyl-D-tryptophan
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-
-
ir
propionyl-CoA + D-allo-isoleucine
CoA + N-propionyl-D-allo-isoleucine
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-
-
-
ir
propionyl-CoA + D-glutamine
CoA + N-propionyl-D-glutamine
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-
-
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ir
propionyl-CoA + D-tryptophan
CoA + N2-propionyl-D-tryptophan
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-
-
ir
acetyl-CoA + a D-amino acid
CoA + an N-acetyl-D-amino acid
-
-
-
-
?
acetyl-CoA + a D-amino acid
CoA + an N-acetyl-D-amino acid
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D-amino acids are toxic to Saccharomyces cerevisiae but are detoxified with D-amino acid-N-acetyltransferase by N-acetylation preceding removal from yeast cells
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-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CoA
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competitive against acetyl-CoA, noncompetitive against D-tryptophan
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brucellosis
The immunomodulatory effect of antimicrobial peptide HPA3P restricts Brucella abortus 544 infection in BALB/c mice.
Colonic Neoplasms
Antitumor activity of HPA3P through RIPK3-dependent regulated necrotic cell death in colon cancer.
Granuloma
The immunomodulatory effect of antimicrobial peptide HPA3P restricts Brucella abortus 544 infection in BALB/c mice.
Infections
The immunomodulatory effect of antimicrobial peptide HPA3P restricts Brucella abortus 544 infection in BALB/c mice.
Neoplasms
Antitumor activity of HPA3P through RIPK3-dependent regulated necrotic cell death in colon cancer.
Neoplasms
The immunomodulatory effect of antimicrobial peptide HPA3P restricts Brucella abortus 544 infection in BALB/c mice.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HPA3_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
161
0
18814
Swiss-Prot
other Location (Reliability: 1)
A0A1D8N8L2_YARLL
150
0
17459
TrEMBL
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
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x * 21000, recombinant intact Hpa3p, SDS-PAGE, x * 18000, recombinant N-terminally truncated enzyme, SDS-PAGE
21000
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x * 21000, recombinant intact Hpa3p, SDS-PAGE, x * 18000, recombinant N-terminally truncated enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 21000, recombinant intact Hpa3p, SDS-PAGE, x * 18000, recombinant N-terminally truncated enzyme, SDS-PAGE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from dry yeast, to homogeneity in several steps, recombinant enzyme from Escherichia coli in a procedure similar to the purification of the native enzyme to 95% purity
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to homogeneity by ammonium sulfate fractionation, DEAE ion exchange chromatography, chromatography on a butyl resin, gel filtration, and D-glutamate affinity chromatography, overview
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
when the gene is overexpressed with a vector plasmid p426Gal1 in the wild type Saccharomyces cerevisiae as a host, the recombinant yeast, which shows more than 100 times higher D-amino acid-N-acetyltransferase activity than the wild type, is much more tolerant to D-amino acids than the wild type
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zenk, M.H.; Schmitt, J.H.
Purification and properties of acetyl-CoA: D-amino acid-alpha-N-acetyltransferase from yeast
Biochem. Z.
342
54-65
1965
Saccharomyces cerevisiae
brenda
Yow, G.Y.; Uo, T.; Yoshimura, T.; Esaki, N.
D-amino acid N-acetyltransferase of Saccharomyces cerevisiae: a close homologue of histone acetyltransferase Hpa2p acting exclusively on free D-amino acids
Arch. Microbiol.
182
396-403
2004
Saccharomyces cerevisiae
brenda
Tashiro, Y.; Tamura, T.; Tanaka, H.; Inagaki, K.
Purification and some properties of D-amino acid acetyltransferase from Saccharomyces cerevisiae
Okayama Daigaku Nogakubu Gakujutsu Hokoku
93
13-18
2004
Saccharomyces cerevisiae
-
brenda
Yow, G.Y.; Uo, T.; Yoshimura, T.; Esaki, N.
Physiological role of D-amino acid-N-acetyltransferase of Saccharomyces cerevisiae: detoxification of D-amino acids
Arch. Microbiol.
185
39-46
2006
Saccharomyces cerevisiae
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