Literature DB >> 11412985

Phenylethanolamine N-methyltransferase kinetics: bovine versus recombinant human enzyme.

G L Grunewald1, M J McLeish, K R Criscione.   

Abstract

Epinephrine (Epi) acts as a neurotransmitter in the brain, but its function therein is not well understood. Phenylethanolamine N-methyltransferase (PNMT) catalyzes the final step in the biosynthesis of Epi and is thus a pharmacological target to investigate the function of Epi in the central nervous system. The kinetic differences between bovine adrenal PNMT and human brain PNMT for a number of substrates and inhibitors are examined and the results reported.

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Year:  2001        PMID： 11412985     DOI： 10.1016/s0960-894x(01)00245-1

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN： 0960-894X            Impact factor:   2.823


  3 in total

1.  Controlling the facial selectivity of asymmetric [4+2] cyclo-additions: a concise synthesis of the cis-decalin core structure of superstolides A and B.

Authors:  Lei Chen; Zhengmao Hua; Gangqin Li; Zhendong Jin
Journal:  Org Lett       Date:  2011-06-14       Impact factor: 6.005

2.  Kinetic and pH studies on human phenylethanolamine N-methyltransferase.

Authors:  Qian Wu; Michael J McLeish
Journal:  Arch Biochem Biophys       Date:  2013-09-07       Impact factor: 4.013

3.  Molecular recognition of physiological substrate noradrenaline by the adrenaline-synthesizing enzyme PNMT and factors influencing its methyltransferase activity.

Authors:  Nyssa Drinkwater; Christine L Gee; Munish Puri; Kevin R Criscione; Michael J McLeish; Gary L Grunewald; Jennifer L Martin
Journal:  Biochem J       Date:  2009-08-27       Impact factor: 3.857
  3 in total

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