Arylamine N-acetyltransferases - of mice, men and microorganisms

@article{citeulike:2732078, abstract = {Arylamine N-acetyltransferases (NATs) catalyse the transfer of an acetyl group from acetyl CoA to the terminal nitrogen of hydrazine and arylamine drugs and carcinogens. These enzymes are polymorphic and have an important place in the history of pharmacogenetics, being first identified as responsible for the polymorphic inactivation of the anti-tubercular drug isoniazid. NAT has recently been identified within Mycobacterium tuberculosis itself and is an important candidate for modulating the response of mycobacteria to isoniazid. The first three-dimensional structure of the unique NAT family shows the active-site cysteine to be aligned with conserved histidine and aspartate residues to form a catalytic triad, thus providing an activation mechanism for transfer of the acetyl group from acetyl CoA to cysteine. The unique fold could allow different members of the NAT family to play a variety of roles in endogenous and xenobiotic metabolism.}, author = {Upton, Anna and Johnson, Nichola and Sandy, James and Sim, Edith }, citeulike-article-id = {2732078}, doi = {http://dx.doi.org/10.1016/S0165-6147(00)01639-4}, journal = {Trends in Pharmacological Sciences}, month = {March}, number = {3}, pages = {140--146}, posted-at = {2008-04-29 07:32:12}, priority = {2}, title = {Arylamine N-acetyltransferases - of mice, men and microorganisms}, url = {http://dx.doi.org/10.1016/S0165-6147(00)01639-4}, volume = {22}, year = {2001} }

TY - JOUR ID - citeulike:2732078 L3 - citeulike-article-id:2732078 TI - Arylamine N-acetyltransferases - of mice, men and microorganisms JF - Trends in Pharmacological Sciences VL - 22 IS - 3 SP - 140 EP - 146 N2 - Arylamine N-acetyltransferases (NATs) catalyse the transfer of an acetyl group from acetyl CoA to the terminal nitrogen of hydrazine and arylamine drugs and carcinogens. These enzymes are polymorphic and have an important place in the history of pharmacogenetics, being first identified as responsible for the polymorphic inactivation of the anti-tubercular drug isoniazid. NAT has recently been identified within Mycobacterium tuberculosis itself and is an important candidate for modulating the response of mycobacteria to isoniazid. The first three-dimensional structure of the unique NAT family shows the active-site cysteine to be aligned with conserved histidine and aspartate residues to form a catalytic triad, thus providing an activation mechanism for transfer of the acetyl group from acetyl CoA to cysteine. The unique fold could allow different members of the NAT family to play a variety of roles in endogenous and xenobiotic metabolism. AU - Upton, Anna AU - Johnson, Nichola AU - Sandy, James AU - Sim, Edith PY - 2001/03/01/ UR - http://dx.doi.org/10.1016/S0165-6147(00)01639-4 ER -