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Literature summary extracted from

  • Fullam, E.; Westwood, I.M.; Anderton, M.C.; Lowe, E.D.; Sim, E.; Noble, M.E.
    Divergence of cofactor recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase (2008), J. Mol. Biol., 375, 178-191.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.5 expressed in Escherichia coli as a His-tagged fusion protein Mycobacterium marinum
2.3.1.5 into the pET28b+ vector for expression in Escherichia coli BL21DE3 pLysS cells Mycobacterium marinum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.5 crystal structure of MMNAT in complex with CoA is determined. The overall MMNAT structure consists of three domains. Domain I forms an alpha-helical bundle (amino acids 4-88), domain II forms a beta-barrel (amino acids 89-200) and domain III forms an alpha/beta lid (amino acids 201-275). Assembled together, the molecular surface of these domains presents a deep and wide active-site cleft, at the base of which is found the catalytic cysteine residue. Surprisingly, the principal CoA recognition site in MMNAT is located some 30 A from the site of CoA recognition in the deposited structure of human NAT2 bound to CoA Mycobacterium marinum
2.3.1.5 the crystal structure of the native enzyme is presented at a resolution of 1.9 A, cocrystallized with CoA at 2.4 A Mycobacterium marinum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.5 0.2
-
5-Aminosalicylate
-
Mycobacterium marinum
2.3.1.5 0.2
-
acetyl-CoA using 5-aminosalicylate as a substrate Mycobacterium marinum

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.5 Mycobacterium marinum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.5 using a Ni-NTA resin Mycobacterium marinum
2.3.1.5 using Ni-NTA chromatography Mycobacterium marinum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.5 additional information
-
MMNAT is found to acetylate a broad range of substrates, including isoniazid, 4-anisidine and 4-aminoveratrole, compounds that have been identified as substrates of the NAT enzyme of Mycobacterium tuberculosis. The specific activity profile differs somewhat from that of the other characterised mycobacterial NAT, NAT from Mycobacterium smegmatis, particularly in the rate of acetylation of hydralazine and 2-aminofluorene, which are both acetylated 100times more rapidly by MMNAT Mycobacterium marinum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.5 acetyl-CoA + 2-aminofluorene
-
Mycobacterium marinum CoA + N-acetyl-2-aminofluorene
-
?
2.3.1.5 acetyl-CoA + 4-aminobenzoic acid
-
Mycobacterium marinum CoA + N-acetyl-4-aminobenzoic acid
-
?
2.3.1.5 acetyl-CoA + 4-aminoveratrole
-
Mycobacterium marinum CoA + N-acetyl-4-aminoveratrole
-
?
2.3.1.5 acetyl-CoA + 4-aminoveratrole
-
Mycobacterium marinum ?
-
?
2.3.1.5 acetyl-CoA + 4-anisidine
-
Mycobacterium marinum CoA + N-acetyl-4-anisidine
-
?
2.3.1.5 acetyl-CoA + 4-bromoaniline
-
Mycobacterium marinum CoA + N-(4-bromophenyl)acetamide
-
?
2.3.1.5 acetyl-CoA + 4-bromoaniline
-
Mycobacterium marinum CoA + N-acetyl-4-bromoaniline
-
?
2.3.1.5 acetyl-CoA + 4-butoxyaniline
-
Mycobacterium marinum CoA + N-acetyl-4-butoxyaniline
-
?
2.3.1.5 acetyl-CoA + 4-butoxyaniline
-
Mycobacterium marinum ?
-
?
2.3.1.5 acetyl-CoA + 4-chloroaniline
-
Mycobacterium marinum CoA + N-acetyl-4-chloroaniline
-
?
2.3.1.5 acetyl-CoA + 4-chloroaniline
-
Mycobacterium marinum CoA + N-(4-chlorophenyl)acetamide
-
?
2.3.1.5 acetyl-CoA + 4-chlorobenzoic hydrazide
-
Mycobacterium marinum ?
-
?
2.3.1.5 acetyl-CoA + 4-chlorobenzoic hydrazide
-
Mycobacterium marinum CoA + N-acetyl-4-chlorobenzoic hydrazide
-
?
2.3.1.5 acetyl-CoA + 4-ethoxyaniline
-
Mycobacterium marinum CoA + N-acetyl-4-ethoxyaniline
-
?
2.3.1.5 acetyl-CoA + 4-ethoxyaniline
-
Mycobacterium marinum ?
-
?
2.3.1.5 acetyl-CoA + 4-hexyloxyaniline
-
Mycobacterium marinum CoA + N-acetyl-4-hexyloxyaniline
-
?
2.3.1.5 acetyl-CoA + 4-hexyloxyaniline
-
Mycobacterium marinum ?
-
?
2.3.1.5 acetyl-CoA + 4-iodoaniline
-
Mycobacterium marinum CoA + N-acetyl-4-iodoaniline
-
?
2.3.1.5 acetyl-CoA + 4-iodoaniline
-
Mycobacterium marinum CoA + N-(4-iodophenyl)acetamide
-
?
2.3.1.5 acetyl-CoA + 4-phenoxyaniline
-
Mycobacterium marinum CoA + N-acetyl-4-phenoxyaniline
-
?
2.3.1.5 acetyl-CoA + 4-phenoxyaniline
-
Mycobacterium marinum ?
-
?
2.3.1.5 acetyl-CoA + 5-aminosalicylate
-
Mycobacterium marinum CoA + N-acetyl-5-aminosalicylate
-
?
2.3.1.5 acetyl-CoA + hydralazine
-
Mycobacterium marinum ?
-
?
2.3.1.5 acetyl-CoA + hydralazine
-
Mycobacterium marinum CoA + N-acetyl-hydralazine
-
?
2.3.1.5 acetyl-CoA + isoniazid
-
Mycobacterium marinum CoA + N-acetyl-isoniazid
-
?
2.3.1.5 acetyl-CoA + isoniazid
-
Mycobacterium marinum ?
-
?
2.3.1.5 acetyl-CoA + p-aminobenzoic acid
-
Mycobacterium marinum CoA + N-acetyl-4-aminobenzoic acid
-
?
2.3.1.5 acetyl-CoA + procainamide
-
Mycobacterium marinum ?
-
?
2.3.1.5 acetyl-CoA + procainamide
-
Mycobacterium marinum CoA + N-acetyl-procainamide
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.5 dimer crystal structure Mycobacterium marinum

Synonyms

EC Number Synonyms Comment Organism
2.3.1.5 arylamine N-acetyltransferase
-
Mycobacterium marinum
2.3.1.5 MMNAT
-
Mycobacterium marinum
2.3.1.5 NAT
-
Mycobacterium marinum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.5 28
-
assay at Mycobacterium marinum
2.3.1.5 28
-
activity assay Mycobacterium marinum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.5 8
-
assay at Mycobacterium marinum
2.3.1.5 8
-
activity assay Mycobacterium marinum

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.5 acetyl-CoA
-
Mycobacterium marinum