Kinetic characterisation of arylamine N-acetyltransferase from Pseudomonas aeruginosa

BMC Biochemistry

Table 6 Summary of Michaelis constants for AcCoA from different NATs.

Enzyme	True or Apparent K_m	Acetyl Acceptor^d	K_m(mM)	Reference
PANAT	Apparent	p-anisidine (0.2 μM)	0.136	[7]
PANAT	Apparent	p-anisidine (2 mM)	0.466 ± 0.077	[see Additional file 2]
PANAT	True	5-AS	1.02 ± 0.29	Table 5
STNAT^a	Apparent	N-OH-Glu-P-1	0.010	[1]
STNAT^a	Apparent	INH	< 0.020	[38]
STNAT - 11^b	Apparent	INH	0.393 ± 0.003	[38]
STNAT - 85^c	Apparent	INH	0.764 ± 0.004	[38]
Pigeon liver NAT	Apparent	p-nitroaniline	0.007	[29]
Hamster NAT2	True	p-nitroaniline, pABA, pABA-Glu	5.94	[35]
Rabbit liver NAT	Apparent	INH	1.5	[26]

Selected Michaelis constants from the literature have been compiled along with those determined in this study for the purified PANAT enzyme.
^aSTNAT, NAT from Salmonella typhimurium.
^bSTNAT truncation mutant, missing 11 amino acids from the C-terminus.
^cSTNAT truncation mutant, missing the entire C-terminal domain (85 amino acids).
^dAbbreviations: 5-AS, 5-aminosalicylic acid; N-OH-Glu-P-1, 2-hydroxyamino-6-methyldipyrido- [1,2-a:3',2'-d]-imidazole; INH, isoniazid; pABA, p-aminobenzoic acid; pABA-Glu, p-aminobenzoyl-L-glutamate.

ISSN: 1471-2091