Literature summary for 2.3.1.258 extracted from

Evjenth, R.H.; Brenner, A.K.; Thompson, P.R.; Arnesen, T.; Fr?ystein, N.A.; Lillehaug, J.R.
Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study (2012), J. Biol. Chem., 287, 10081-10088.

Search for more literature for 2.3.1.258

Protein Variants

Protein Variants	Comment	Organism
H112A	inactive	Homo sapiens
H112A	NMR spectroscopy using the catalytically inactive hNaa50p mutant	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
CoA	competitive product inhibition; product inhibition, competitive versus acetyl-CoA, noncompetitive against peptide substrate well in line with a ternary complex mechanism. The non-competitive inhibition pattern observed when CoA is tested against peptide as variable substrate and at fixed concentrations of acetyl-CoA also rules out a ping-pong mechanism	Homo sapiens
desulfo-CoA	competitive inhibition; competitive versus acetyl-CoA	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	steady-state kinetics, overview	Homo sapiens
0.005	-	acetyl-CoA	pH 7.4, temperature not specified in the publication	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetyl-CoA + peptide	Homo sapiens	-	CoA + Nalpha-acetylpeptide	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Homo sapiens	Q9GZZ1	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA	hNaa50p utilizes an ordered bi bi reaction of the Theorell-Chance type, substarte binding study and dynamics using NMR spectroscopy. Acetyl-CoA induces a conformational change that is required for the peptide to bind to the active site. Addition of peptide in the absence of acetyl-CoA does not alter the structure of the protein	Homo sapiens	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + MLGPEGGRWGRPVGRRRRPVRVYP	optimal in vitro substrate	Homo sapiens	?	-	?
acetyl-CoA + peptide	-	Homo sapiens	CoA + Nalpha-acetylpeptide	-	?
additional information	Naa50p also possesses Nepsilon-autoacetylation activity	Homo sapiens	?	-	?

Synonyms

Synonyms	Comment	Organism
Naa50p	-	Homo sapiens
NAT5/SAN	-	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	8	assay at	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
acetyl-CoA	acetyl-CoA induces a conformational change that is required for the peptide to bind to the active site	Homo sapiens

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.00227	-	CoA	with acetyl-CoA, pH 7.4, temperature not specified in the publication	Homo sapiens
0.0027	-	CoA	pH and temperature not specified in the publication	Homo sapiens
0.00277	-	CoA	with peptide, pH 7.4, temperature not specified in the publication	Homo sapiens
0.067	-	desulfo-CoA	pH and temperature not specified in the publication	Homo sapiens
0.067	-	desulfo-CoA	with acetyl-CoA, pH 7.4, temperature not specified in the publication	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)