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PMID: 3541912 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase.

The Biochemical journal ·Vol. 238 ·No. 2 ·1986-09-01 ·Pages 475-83

Duncan K, Chaudhuri S, Campbell MS, Coggins JR

Abstract

The enzyme 3-dehydroquinase was purified in milligram quantities from an overproducing strain of Escherichia coli. The amino acid sequence was deduced from the nucleotide sequence of the aroD gene and confirmed by determining the amino acid composition of the overproduced enzyme and its N-terminal amino acid sequence. The complete polypeptide chain consists of 240 amino acid residues and has a calculated subunit Mr of 26,377. Transcript mapping revealed that aroD is a typical monocistronic gene.

MeSH Terms
Amino Acid Sequence Base Sequence Cloning, Molecular Codon/genetics DNA, Bacterial/genetics Escherichia coli/enzymology,genetics Hydro-Lyases/genetics Transcription, Genetic
Chemicals
Codon DNA, Bacterial Hydro-Lyases 3-dehydroquinate dehydratase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Duncan K
Chaudhuri S
Campbell M S
Coggins J R
References (35)
35 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2380475
Published
1986-09-01
Pages
475-83
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1147159
Subset
IM
Databases
GENBANK
X04306
External Links
PubMed source DOI: 10.1042/bj2380475 PMC Full Text View journal details
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