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Title: Carotenoid biosynthesis in bacteria: In vitro studies of a crt/bch transcription factor from Rhodobacter capsulatus and carotenoid enzymes from Erwinia herbicola

Abstract

A putative transcription factor in Rhodobactor capsulatus which binds upstream of the crt and bch pigment biosynthesis operons and appears to play a role in the adaptation of the organism from the aerobic to the anaerobic-photosynthetic growth mode was characterized. Chapter 2 describes the identification of this factor through an in vitro mobility shift assay, as well as the determination of its binding properties and sequence specificity. Chapter 3 focuses on the isolation of this factor. Biochemistry of later carotenoid biosynthesis enzymes derived from the non-photosynthetic bacterium, Erwinia herbicola. Chapter 4 describes the separate overexpression and in vitro analysis of two enzymes involved in the main sequence of the carotenoid biosynthesis pathway, lycopene cyclase and 5-carotene hydroxylase. Chapter 5 examines the overexpression and enzymology of functionally active zeaxanthin glucosyltransferase, an enzyme which carries out a more unusual transformation, converting a carotenoid into its more hydrophilic mono- and diglucoside derivatives. In addition, amino acid homology with other glucosyltransferases suggests a putative binding site for the UDP-activated glucose substrate.

Authors:
Publication Date:
Research Org.:
Lawrence Berkeley Lab., CA (United States)
Sponsoring Org.:
DOE; USDOE, Washington, DC (United States)
OSTI Identifier:
6880113
Alternate Identifier(s):
OSTI ID: 6880113; Legacy ID: DE93010409
Report Number(s):
LBL-33496
ON: DE93010409
DOE Contract Number:  
AC03-76SF00098
Resource Type:
Technical Report
Resource Relation:
Other Information: Thesis (Ph.D.)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 14 SOLAR ENERGY; CAROTENOIDS; BIOSYNTHESIS; CYCLASES; GENE REGULATION; GENE REPRESSORS; BIOCHEMICAL REACTION KINETICS; GLYCOSYL TRANSFERASES; TRANSCRIPTION FACTORS; PHOTOSYNTHETIC BACTERIA; ENZYMES; HYDROCARBONS; KINETICS; LYASES; ORGANIC COMPOUNDS; PIGMENTS; PROTEINS; REACTION KINETICS; SYNTHESIS; TERPENES; TRANSFERASES 550200* -- Biochemistry; 550500 -- Metabolism; 140505 -- Solar Energy Conversion-- Photochemical, Photobiological, & Thermochemical Conversion-- (1980-)

Citation Formats

O'Brien, D.A.. Carotenoid biosynthesis in bacteria: In vitro studies of a crt/bch transcription factor from Rhodobacter capsulatus and carotenoid enzymes from Erwinia herbicola. United States: N. p., 1992. Web. doi:10.2172/6880113.
O'Brien, D.A.. Carotenoid biosynthesis in bacteria: In vitro studies of a crt/bch transcription factor from Rhodobacter capsulatus and carotenoid enzymes from Erwinia herbicola. United States. doi:10.2172/6880113.
O'Brien, D.A.. Sun . "Carotenoid biosynthesis in bacteria: In vitro studies of a crt/bch transcription factor from Rhodobacter capsulatus and carotenoid enzymes from Erwinia herbicola". United States. doi:10.2172/6880113. https://www.osti.gov/servlets/purl/6880113.
@article{osti_6880113,
title = {Carotenoid biosynthesis in bacteria: In vitro studies of a crt/bch transcription factor from Rhodobacter capsulatus and carotenoid enzymes from Erwinia herbicola},
author = {O'Brien, D.A.},
abstractNote = {A putative transcription factor in Rhodobactor capsulatus which binds upstream of the crt and bch pigment biosynthesis operons and appears to play a role in the adaptation of the organism from the aerobic to the anaerobic-photosynthetic growth mode was characterized. Chapter 2 describes the identification of this factor through an in vitro mobility shift assay, as well as the determination of its binding properties and sequence specificity. Chapter 3 focuses on the isolation of this factor. Biochemistry of later carotenoid biosynthesis enzymes derived from the non-photosynthetic bacterium, Erwinia herbicola. Chapter 4 describes the separate overexpression and in vitro analysis of two enzymes involved in the main sequence of the carotenoid biosynthesis pathway, lycopene cyclase and 5-carotene hydroxylase. Chapter 5 examines the overexpression and enzymology of functionally active zeaxanthin glucosyltransferase, an enzyme which carries out a more unusual transformation, converting a carotenoid into its more hydrophilic mono- and diglucoside derivatives. In addition, amino acid homology with other glucosyltransferases suggests a putative binding site for the UDP-activated glucose substrate.},
doi = {10.2172/6880113},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Sun Nov 01 00:00:00 EST 1992},
month = {Sun Nov 01 00:00:00 EST 1992}
}

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