MECHANISM OP ACTION OP p-HYDROXYBENZOATE HYBROZYLASE FROMPseudomonas putida. III. THE ENZYME-SUBTRATE COMPLEX

PDF Version Also Available for Download.

Description

The mechanism of action of p-hydroxybenzoate hydroxylase from Pseudomonas putida, strain M-6, has been investigated. The aromatic substrate analogues, benzoate, p-fluorobenzoate, p-chlorobenzoate, p-nitrobenzoate, p-aminobenzoate, and 6-hydroxynicotinate, are found to be competitive inhibitors. This finding differs from the previously reported noncompetitive behavior in a different buffer system. The optical activity of the enzyme-inhibitor complex is studied. From the kinetic and circular dichroism (CD) measurements, they have found that the carboxyl moiety is necessary and sufficient for the enzyme-substrate binding, whereas the hydroxyl group alone will not lead to binding. There are two classes of inhibitory analogues: one causes changes in CD ... continued below

Physical Description

32 p.

Creation Information

Teng, Nelson N.H.; Kbtovycz, George.; Calvin, Melvin. & Hosokawa,Keiichi. April 1, 1971.

Context

This report is part of the collection entitled: Office of Scientific & Technical Information Technical Reports and was provided by UNT Libraries Government Documents Department to Digital Library, a digital repository hosted by the UNT Libraries. More information about this report can be viewed below.

Who

People and organizations associated with either the creation of this report or its content.

Publisher

Provided By

UNT Libraries Government Documents Department

Serving as both a federal and a state depository library, the UNT Libraries Government Documents Department maintains millions of items in a variety of formats. The department is a member of the FDLP Content Partnerships Program and an Affiliated Archive of the National Archives.

Contact Us

What

Descriptive information to help identify this report. Follow the links below to find similar items on the Digital Library.

Description

The mechanism of action of p-hydroxybenzoate hydroxylase from Pseudomonas putida, strain M-6, has been investigated. The aromatic substrate analogues, benzoate, p-fluorobenzoate, p-chlorobenzoate, p-nitrobenzoate, p-aminobenzoate, and 6-hydroxynicotinate, are found to be competitive inhibitors. This finding differs from the previously reported noncompetitive behavior in a different buffer system. The optical activity of the enzyme-inhibitor complex is studied. From the kinetic and circular dichroism (CD) measurements, they have found that the carboxyl moiety is necessary and sufficient for the enzyme-substrate binding, whereas the hydroxyl group alone will not lead to binding. There are two classes of inhibitory analogues: one causes changes in CD spectra of the enzyme similar to those evoked by the substrate, and the other does not cause significant changes. the results indicate that more than one mode of enzyme-inhibitor interaction is involved. The CD of the enzyme-NADPH complex under anaerobic conditions suggests that the oxidized enzyme and reduced pyridine nucleotide form a complex, both in the absence and presence of the substrate, p-hydroxybenzoate. Furthermore, evidence for a ternary complex is given.

Physical Description

32 p.

Language

Item Type

Identifier

Unique identifying numbers for this report in the Digital Library or other systems.

  • Report No.: UCRL--20651
  • Grant Number: DE-AC02-05CH11231
  • DOI: 10.2172/928503 | External Link
  • Office of Scientific & Technical Information Report Number: 928503
  • Archival Resource Key: ark:/67531/metadc898995

Collections

This report is part of the following collection of related materials.

Office of Scientific & Technical Information Technical Reports

Reports, articles and other documents harvested from the Office of Scientific and Technical Information.

Office of Scientific and Technical Information (OSTI) is the Department of Energy (DOE) office that collects, preserves, and disseminates DOE-sponsored research and development (R&D) results that are the outcomes of R&D projects or other funded activities at DOE labs and facilities nationwide and grantees at universities and other institutions.

What responsibilities do I have when using this report?

When

Dates and time periods associated with this report.

Creation Date

  • April 1, 1971

Added to The UNT Digital Library

  • Sept. 27, 2016, 1:39 a.m.

Description Last Updated

  • Nov. 3, 2016, 8:12 p.m.

Usage Statistics

When was this report last used?

Yesterday: 0
Past 30 days: 0
Total Uses: 8

Interact With This Report

Here are some suggestions for what to do next.

Start Reading

PDF Version Also Available for Download.

International Image Interoperability Framework

IIF Logo

We support the IIIF Presentation API

Teng, Nelson N.H.; Kbtovycz, George.; Calvin, Melvin. & Hosokawa,Keiichi. MECHANISM OP ACTION OP p-HYDROXYBENZOATE HYBROZYLASE FROMPseudomonas putida. III. THE ENZYME-SUBTRATE COMPLEX, report, April 1, 1971; Berkeley, California. (digital.library.unt.edu/ark:/67531/metadc898995/: accessed September 24, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.