Examination of N-hydroxylation as a prerequisite mechanism of nitric oxide synthase inactivation

Tristan S. Maurer; Jianping Pan; Brian P. Booth; Thomas I. Kalman; Ho Leung Fung

doi:10.1016/S0960-894X(00)00171-2

Examination of N-hydroxylation as a prerequisite mechanism of nitric oxide synthase inactivation

Tristan S. Maurer
, Jianping Pan
, Brian P. Booth
, Thomas I. Kalman
, Ho Leung Fung

SUNY Buffalo

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

L-N⁵-(1-Hydroxyiminoethyl)-ornithine (L-NHIO) and L-N⁶-(1-hydroxyiminoethyl)-lysine (L-NHIL) were synthesized and tested as potential intermediates in the mechanism-based inactivation of nitric oxide synthase (NOS) by L-N⁵-iminoethyl-ornithine (L-NIO) and L-N⁶-iminoethyllysine (L-NIL). Although these compounds were determined to be competitive inhibitors, mechanism-based inactivation was not observed. (C) 2000 Elsevier Science Ltd. All rights reserved.

Original language	English
Pages (from-to)	1077-1080
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	10
Issue number	10
DOIs	https://doi.org/10.1016/S0960-894X(00)00171-2
State	Published - May 15 2000

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title = "Examination of N-hydroxylation as a prerequisite mechanism of nitric oxide synthase inactivation",

abstract = "L-N5-(1-Hydroxyiminoethyl)-ornithine (L-NHIO) and L-N6-(1-hydroxyiminoethyl)-lysine (L-NHIL) were synthesized and tested as potential intermediates in the mechanism-based inactivation of nitric oxide synthase (NOS) by L-N5-iminoethyl-ornithine (L-NIO) and L-N6-iminoethyllysine (L-NIL). Although these compounds were determined to be competitive inhibitors, mechanism-based inactivation was not observed. (C) 2000 Elsevier Science Ltd. All rights reserved.",

author = "Maurer, \{Tristan S.\} and Jianping Pan and Booth, \{Brian P.\} and Kalman, \{Thomas I.\} and Fung, \{Ho Leung\}",

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T1 - Examination of N-hydroxylation as a prerequisite mechanism of nitric oxide synthase inactivation

AU - Maurer, Tristan S.

AU - Pan, Jianping

AU - Booth, Brian P.

AU - Kalman, Thomas I.

AU - Fung, Ho Leung

PY - 2000/5/15

Y1 - 2000/5/15

N2 - L-N5-(1-Hydroxyiminoethyl)-ornithine (L-NHIO) and L-N6-(1-hydroxyiminoethyl)-lysine (L-NHIL) were synthesized and tested as potential intermediates in the mechanism-based inactivation of nitric oxide synthase (NOS) by L-N5-iminoethyl-ornithine (L-NIO) and L-N6-iminoethyllysine (L-NIL). Although these compounds were determined to be competitive inhibitors, mechanism-based inactivation was not observed. (C) 2000 Elsevier Science Ltd. All rights reserved.

AB - L-N5-(1-Hydroxyiminoethyl)-ornithine (L-NHIO) and L-N6-(1-hydroxyiminoethyl)-lysine (L-NHIL) were synthesized and tested as potential intermediates in the mechanism-based inactivation of nitric oxide synthase (NOS) by L-N5-iminoethyl-ornithine (L-NIO) and L-N6-iminoethyllysine (L-NIL). Although these compounds were determined to be competitive inhibitors, mechanism-based inactivation was not observed. (C) 2000 Elsevier Science Ltd. All rights reserved.

UR - https://www.scopus.com/pages/publications/0034658090

U2 - 10.1016/S0960-894X(00)00171-2

DO - 10.1016/S0960-894X(00)00171-2

M3 - Article

C2 - 10843221

AN - SCOPUS:0034658090

SN - 0960-894X

VL - 10

SP - 1077

EP - 1080

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 10

ER -

Examination of N-hydroxylation as a prerequisite mechanism of nitric oxide synthase inactivation

Abstract

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