Mechanism-based inactivation of L-pipecolate oxidase by a sulfur-containing substrate analog, 5-THIA-L-pipecolic acid

T. Mark Zabriskie; Xi Liang

doi:10.1016/S0960-894X(97)00042-5

Mechanism-based inactivation of L-pipecolate oxidase by a sulfur-containing substrate analog, 5-THIA-L-pipecolic acid

T. Mark Zabriskie, Xi Liang

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

4 Scopus citations

Abstract

5-Thia-L-pipecolic acid, (S)-1,3-thiazane-4-carboxylic acid (6), was synthesized and found to serve as an excellent substrate for Rhesus monkey liver L-pipecolate oxidase (L-PO) and also to cause time-dependent, irreversible inactivation of the enzyme. Data are presented demonstrating 6 is a mechanism-based inactivator of L-PO and one of the enzyme turnover products is identified as homocysteine.

Original language	English (US)
Pages (from-to)	457-462
Number of pages	6
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	7
Issue number	4
DOIs	https://doi.org/10.1016/S0960-894X(97)00042-5
State	Published - Feb 18 1997
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

Access to Document

10.1016/S0960-894X(97)00042-5

Cite this

@article{258c33e6a4d7408094bbc3ccbffb0b48,

title = "Mechanism-based inactivation of L-pipecolate oxidase by a sulfur-containing substrate analog, 5-THIA-L-pipecolic acid",

abstract = "5-Thia-L-pipecolic acid, (S)-1,3-thiazane-4-carboxylic acid (6), was synthesized and found to serve as an excellent substrate for Rhesus monkey liver L-pipecolate oxidase (L-PO) and also to cause time-dependent, irreversible inactivation of the enzyme. Data are presented demonstrating 6 is a mechanism-based inactivator of L-PO and one of the enzyme turnover products is identified as homocysteine.",

author = "Zabriskie, {T. Mark} and Xi Liang",

note = "Funding Information: Acknowledgment: This work is supportedb y grantsf rom the NationalI nstitutefo r NeurologicaDl isorders and Stroke( NS 32421)a ndthe MedicalR esearchF oundationo f Oregon.P rimatet issueu sedin theses tudies was obtainedfr omthe OregonR egionaPl rimateR esearchC enterw hichis supportebdy NIH GrantR R 00163.",

year = "1997",

month = feb,

day = "18",

doi = "10.1016/S0960-894X(97)00042-5",

language = "English (US)",

volume = "7",

pages = "457--462",

journal = "Bioorganic and Medicinal Chemistry Letters",

issn = "0960-894X",

publisher = "Elsevier Limited",

number = "4",

}

TY - JOUR

T1 - Mechanism-based inactivation of L-pipecolate oxidase by a sulfur-containing substrate analog, 5-THIA-L-pipecolic acid

AU - Zabriskie, T. Mark

AU - Liang, Xi

N1 - Funding Information: Acknowledgment: This work is supportedb y grantsf rom the NationalI nstitutefo r NeurologicaDl isorders and Stroke( NS 32421)a ndthe MedicalR esearchF oundationo f Oregon.P rimatet issueu sedin theses tudies was obtainedfr omthe OregonR egionaPl rimateR esearchC enterw hichis supportebdy NIH GrantR R 00163.

PY - 1997/2/18

Y1 - 1997/2/18

N2 - 5-Thia-L-pipecolic acid, (S)-1,3-thiazane-4-carboxylic acid (6), was synthesized and found to serve as an excellent substrate for Rhesus monkey liver L-pipecolate oxidase (L-PO) and also to cause time-dependent, irreversible inactivation of the enzyme. Data are presented demonstrating 6 is a mechanism-based inactivator of L-PO and one of the enzyme turnover products is identified as homocysteine.

AB - 5-Thia-L-pipecolic acid, (S)-1,3-thiazane-4-carboxylic acid (6), was synthesized and found to serve as an excellent substrate for Rhesus monkey liver L-pipecolate oxidase (L-PO) and also to cause time-dependent, irreversible inactivation of the enzyme. Data are presented demonstrating 6 is a mechanism-based inactivator of L-PO and one of the enzyme turnover products is identified as homocysteine.

UR - http://www.scopus.com/inward/record.url?scp=0031576832&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031576832&partnerID=8YFLogxK

U2 - 10.1016/S0960-894X(97)00042-5

DO - 10.1016/S0960-894X(97)00042-5

M3 - Article

AN - SCOPUS:0031576832

SN - 0960-894X

VL - 7

SP - 457

EP - 462

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 4

ER -

Mechanism-based inactivation of L-pipecolate oxidase by a sulfur-containing substrate analog, 5-THIA-L-pipecolic acid

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this