Identification of the Intersubunit Binding Region in Rat Tyrosine Hydroxylase

D. L. Lohse, Paul F Fitzpatrick

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Limited proteolysis converts the 39200 molecular weight catalytic domain of rat tyrosine hydroxylase to a monomer with a molecular weight of 37600. The purified monomer is almost fully active, with minor changes in kinetic parameters at pH 7. Mass spectral analysis and N-terminal sequencing of the proteolytically generated species establish that 20 amino acids have been removed from the carboxyl terminus and five from the amino terminus. Based on these results, the carboxyl terminus is responsible for tetramer formation by tyrosine hydroxylase. The sequence of amino acids which is removed is consistent with a coiled coil structure in the intact tetramer.

Original languageEnglish (US)
Pages (from-to)1543-1548
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume197
Issue number3
DOIs
StatePublished - Dec 30 1993
Externally publishedYes

Fingerprint

Tyrosine 3-Monooxygenase
Rats
Monomers
Molecular Weight
Molecular weight
Proteolysis
Amino Acids
Kinetic parameters
Spectrum analysis
Amino Acid Sequence
Catalytic Domain

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

Identification of the Intersubunit Binding Region in Rat Tyrosine Hydroxylase. / Lohse, D. L.; Fitzpatrick, Paul F.

In: Biochemical and Biophysical Research Communications, Vol. 197, No. 3, 30.12.1993, p. 1543-1548.

Research output: Contribution to journalArticle

@article{6079117f37ed43d898339436f173ed1e,
title = "Identification of the Intersubunit Binding Region in Rat Tyrosine Hydroxylase",
abstract = "Limited proteolysis converts the 39200 molecular weight catalytic domain of rat tyrosine hydroxylase to a monomer with a molecular weight of 37600. The purified monomer is almost fully active, with minor changes in kinetic parameters at pH 7. Mass spectral analysis and N-terminal sequencing of the proteolytically generated species establish that 20 amino acids have been removed from the carboxyl terminus and five from the amino terminus. Based on these results, the carboxyl terminus is responsible for tetramer formation by tyrosine hydroxylase. The sequence of amino acids which is removed is consistent with a coiled coil structure in the intact tetramer.",
author = "Lohse, {D. L.} and Fitzpatrick, {Paul F}",
year = "1993",
month = "12",
day = "30",
doi = "10.1006/bbrc.1993.2653",
language = "English (US)",
volume = "197",
pages = "1543--1548",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Identification of the Intersubunit Binding Region in Rat Tyrosine Hydroxylase

AU - Lohse, D. L.

AU - Fitzpatrick, Paul F

PY - 1993/12/30

Y1 - 1993/12/30

N2 - Limited proteolysis converts the 39200 molecular weight catalytic domain of rat tyrosine hydroxylase to a monomer with a molecular weight of 37600. The purified monomer is almost fully active, with minor changes in kinetic parameters at pH 7. Mass spectral analysis and N-terminal sequencing of the proteolytically generated species establish that 20 amino acids have been removed from the carboxyl terminus and five from the amino terminus. Based on these results, the carboxyl terminus is responsible for tetramer formation by tyrosine hydroxylase. The sequence of amino acids which is removed is consistent with a coiled coil structure in the intact tetramer.

AB - Limited proteolysis converts the 39200 molecular weight catalytic domain of rat tyrosine hydroxylase to a monomer with a molecular weight of 37600. The purified monomer is almost fully active, with minor changes in kinetic parameters at pH 7. Mass spectral analysis and N-terminal sequencing of the proteolytically generated species establish that 20 amino acids have been removed from the carboxyl terminus and five from the amino terminus. Based on these results, the carboxyl terminus is responsible for tetramer formation by tyrosine hydroxylase. The sequence of amino acids which is removed is consistent with a coiled coil structure in the intact tetramer.

UR - http://www.scopus.com/inward/record.url?scp=0027715957&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027715957&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1993.2653

DO - 10.1006/bbrc.1993.2653

M3 - Article

C2 - 7904160

AN - SCOPUS:0027715957

VL - 197

SP - 1543

EP - 1548

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -