Characterization of a key trifunctional enzyme for aromatic amino acid biosynthesis in Archaeoglobus fulgidus

In the aromatic amino acid biosynthesis pathway, chorismate presents a branch point intermediate that is converted to tryptophan, phenylalanine (Phe), and tyrosine (Tyr). In bacteria, three enzymes catalyze the conversion of chorismate to hydroxyphenylpyruvate or pyruvate. The enzymes, chorismate mu...

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Bibliographic Details
Published in:Extremophiles : life under extreme conditions Vol. 13; no. 1; pp. 191 - 198
Main Authors: Lim, Sierin, Springstead, James R, Yu, Marcella, Bartkowski, Wojciech, Schröder, Imke, Monbouquette, Harold G
Format: Journal Article
Language:English
Published: Japan Japan : Springer Japan 2009
Springer Japan
Springer
Springer Nature B.V
Subjects:
Amino acids
Amino Acids, Aromatic - biosynthesis
Archaeoglobus fulgidus
Archaeoglobus fulgidus - enzymology
Archaeoglobus fulgidus - genetics
Bacteria
Bacteriology
Base Sequence
Biochemistry
Biological and medical sciences
Biomedical and Life Sciences
Biosynthesis
Biotechnology
Chromatography, Liquid
DNA Primers
E coli
Electrophoresis, Polyacrylamide Gel
Enzymes
Escherichia coli
Fundamental and applied biological sciences. Psychology
Kinetics
Life Sciences
Mass Spectrometry
Metabolism. Enzymes
Metabolites
Microbial Ecology
Microbiology
Nanoarchaeum equitans
Original Paper
Phylogeny
Polymerase Chain Reaction
Proteins
Thermodynamics
Evolution
Aromatic amino acid biosynthesis
Chorismate mutase
Prephenate dehydratase
Prephenate dehydrogenase
Archaea
Archaeoglobus
Archaeobacteria
Enzyme
Archaeoglobus fulgidus
Lyases
Biosynthesis
Characterization
Isomerases
Gene
Aminoacid
Intramolecular transferases
Bacteria
Aromatic compound
Oxidoreductases
Molecular cloning
Carbon-oxygen lyases
Extreme environment
Hydro-lyases
ISSN:1431-0651, 1433-4909, 1433-4909
Online Access:Get full text
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Summary:In the aromatic amino acid biosynthesis pathway, chorismate presents a branch point intermediate that is converted to tryptophan, phenylalanine (Phe), and tyrosine (Tyr). In bacteria, three enzymes catalyze the conversion of chorismate to hydroxyphenylpyruvate or pyruvate. The enzymes, chorismate mutase (CM), prephenate dehydratase (PDT), and prephenate dehydrogenase (PDHG) are either present as distinct proteins or fusions combining two activities. Gene locus AF0227 of Archaeoglobus fulgidus is predicted to encode a fusion protein, AroQ, containing all three enzymatic domains. This work describes the first characterization of a trifunctional AroQ. The A. fulgidus aroQ gene was cloned and overexpressed in Escherichia coli. The recombinant protein purified as a homohexamer with specific activities of 10, 0.51, and 50 U/mg for CM, PDT, and PDHG, respectively. Tyr at 0.5 mM concentration inhibited PDHG activity by 50%, while at 1 mM PDT was activated by 70%. Phe at 5 μM inhibited PDT activity by 66% without affecting the activity of PDHG. A fusion of CM, PDT, and PDHG domains is evident in the genome of only one other organism sequenced to date, that of the hyperthermophilic archaeon, Nanoarchaeum equitans. Such fusions of contiguous activities in a biosynthetic pathway may constitute a primitive strategy for the efficient processing of labile metabolites.
Bibliography:http://dx.doi.org/10.1007/s00792-008-0209-z
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ISSN:1431-0651
1433-4909
1433-4909
DOI:10.1007/s00792-008-0209-z