The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor

P.J. White; John Ding E. Young; I.S. Hunter; H.G. Nimmo; J.R. Coggins

The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor

P.J. White, John Ding E. Young, I.S. Hunter, H.G. Nimmo, J.R. Coggins

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

Abstract

The enzyme 3-dehydroquinase was purified over 4000-fold to homogeneity from Streptomyces coelicolor. The subunit M(r) estimated from polyacrylamide-gel electrophoresis in the presence of SDS was 16,000. The native M(r) estimated by gel filtration on a Superose 6 column was 209,000, indicating that the enzyme is a large oligomer. The enzyme was found to be extremely thermostable. This stability, along with the structural and kinetic properties of the enzyme, suggest that it is very similar to the quinate-inducible 3-dehydroquinase found in Neurospora crassa and Aspergillus nidulans. This similarity was confirmed by direct N-terminal sequencing.

Original language	American English
Pages (from-to)	735-738
Journal	Biochemical Journal
Volume	265
Issue number	3
State	Published - 1990

Keywords

Amino Acid Sequence
Chromatography, Liquid
Electrophoresis, Polyacrylamide Gel
Hydro-Lyases
Molecular Sequence Data
Streptomyces
Support, Non-U.S. Gov't
Uroporphyrins

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title = "The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor",

abstract = "The enzyme 3-dehydroquinase was purified over 4000-fold to homogeneity from Streptomyces coelicolor. The subunit M(r) estimated from polyacrylamide-gel electrophoresis in the presence of SDS was 16,000. The native M(r) estimated by gel filtration on a Superose 6 column was 209,000, indicating that the enzyme is a large oligomer. The enzyme was found to be extremely thermostable. This stability, along with the structural and kinetic properties of the enzyme, suggest that it is very similar to the quinate-inducible 3-dehydroquinase found in Neurospora crassa and Aspergillus nidulans. This similarity was confirmed by direct N-terminal sequencing.",

keywords = "Amino Acid Sequence, Chromatography, Liquid, Electrophoresis, Polyacrylamide Gel, Hydro-Lyases, Molecular Sequence Data, Streptomyces, Support, Non-U.S. Gov't, Uroporphyrins",

author = "P.J. White and Young, {John Ding E.} and I.S. Hunter and H.G. Nimmo and J.R. Coggins",

year = "1990",

language = "American English",

volume = "265",

pages = "735--738",

journal = "Biochemical Journal",

issn = "0264-6021",

publisher = "Portland Press Ltd",

number = "3",

}

TY - JOUR

T1 - The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor

AU - White, P.J.

AU - Young, John Ding E.

AU - Hunter, I.S.

AU - Nimmo, H.G.

AU - Coggins, J.R.

PY - 1990

Y1 - 1990

N2 - The enzyme 3-dehydroquinase was purified over 4000-fold to homogeneity from Streptomyces coelicolor. The subunit M(r) estimated from polyacrylamide-gel electrophoresis in the presence of SDS was 16,000. The native M(r) estimated by gel filtration on a Superose 6 column was 209,000, indicating that the enzyme is a large oligomer. The enzyme was found to be extremely thermostable. This stability, along with the structural and kinetic properties of the enzyme, suggest that it is very similar to the quinate-inducible 3-dehydroquinase found in Neurospora crassa and Aspergillus nidulans. This similarity was confirmed by direct N-terminal sequencing.

AB - The enzyme 3-dehydroquinase was purified over 4000-fold to homogeneity from Streptomyces coelicolor. The subunit M(r) estimated from polyacrylamide-gel electrophoresis in the presence of SDS was 16,000. The native M(r) estimated by gel filtration on a Superose 6 column was 209,000, indicating that the enzyme is a large oligomer. The enzyme was found to be extremely thermostable. This stability, along with the structural and kinetic properties of the enzyme, suggest that it is very similar to the quinate-inducible 3-dehydroquinase found in Neurospora crassa and Aspergillus nidulans. This similarity was confirmed by direct N-terminal sequencing.

KW - Amino Acid Sequence

KW - Chromatography, Liquid

KW - Electrophoresis, Polyacrylamide Gel

KW - Hydro-Lyases

KW - Molecular Sequence Data

KW - Streptomyces

KW - Support, Non-U.S. Gov't

KW - Uroporphyrins

M3 - Journal Article

C2 - 2306211

SN - 0264-6021

VL - 265

SP - 735

EP - 738

JO - Biochemical Journal

JF - Biochemical Journal

IS - 3

ER -

The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor

Abstract

Keywords

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