NDLI: Subunit structure of a class A aspartate transcarbamoylase from Pseudomonas fluorescens.

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Subunit structure of a class A aspartate transcarbamoylase from Pseudomonas fluorescens.

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Subunit structure of a class A aspartate transcarbamoylase from Pseudomonas fluorescens.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bergh, S. T. Evans, D. R.
Description	Author Affiliation: Bergh ST ( Department of Biochemistry, Wayne State University School of Medicine, Detroit, MI 48201.);
Abstract	The class A aspartate transcarbamoylase (ATCase, EC 2.1.3.2) from Pseudomonas fluorescens was purified to homogeneity with retention of full catalytic and regulatory functions. Careful determinations under conditions that minimized proteolysis showed that the molecule is a 1:1 stoichiometric complex of two polypeptide chains of 34 and 45 kDa. Pyridoxal phosphate is a competitive inhibitor of the enzyme (Ki = 1 microM). Reduction of the pyridoxal phosphate enzyme adduct with sodium boro[3H]hydride showed that the active site is located on the 34-kDa polypeptide. Affinity labeling with 5'-[p-(fluorosulfonyl)benzoyl]adenosine, an ATP analog, suggested that the regulatory site is also located on the 34-kDa species. While the function of the 45-kDa subunit is unknown, neither carbamoyl phosphate synthetase nor dihydroorotase activities are associated with the ATCase. The molecular mass of the enzyme was determined by gel filtration, sedimentation velocity, and electron microscopy to be 464 kDa. Thus the enzyme is composed of six copies of the 34-kDa polypeptide and six copies of the 45-kDa polypeptide. The molecule has a Stokes' ratio of 70.9 A and a frictional ratio of 1.37, suggesting a compact globular shape. We propose that the P. fluorescens ATCase is composed of two trimers of 34-kDa catalytic chains and is likely to be a D3 dodecamer with an arrangement of subunits analogous to that of the class B ATCase molecules.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	90
Language	English
Publisher	National Academy of Sciences
Publisher Date	1993-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aspartate Carbamoyltransferase Chemistry Pseudomonas Fluorescens Enzymology Amino Acid Sequence Isolation & Purification Metabolism Chromatography Chromatography, Gel Durapatite Electrophoresis, Polyacrylamide Gel Kinetics Macromolecular Substances Molecular Sequence Data Molecular Weight Peptide Fragments Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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