Crystallographic and biochemical analysis of three distinct hydrolases : Dermatophagoides pteronyssinus 1 (Der p1), momordin and the bacterial carbon-carbon hydrolase, MhpC
Crystallographic and biochemical analysis of three distinct hydrolases : Dermatophagoides pteronyssinus 1 (Der p1), momordin and the bacterial carbon-carbon hydrolase, MhpC
MhpC is one of six enzymes derived from the mhp operon, which collectively give rise to meta-cleavage pathway for the degradation of 3-(3-hydroxyphenyl)propionic acids (3-HPP) in Escherichia coli. These enzymes work in tandem to convert 3-HPP to metabolites which can then be fed into the Kreb's cycle for energy release. The role of MhpC in this pathway is to convert 2-hydroxy-6-ketonona-2,4-diene-1,9-dioate to 2-hydroxy-penta-2, 4-dienoate and succinate. This reaction involves the breaking of a carbon-carbon bond, which constitutes a rare catalytic event in nature. Elucidating the catalytic mechanism of MhpC will provide invaluable information at the molecular level contributing to the understanding of how biodegradation of environmental pollutants can be achieved.
The MhpC structure has been solved using Multiwavelength Anomalous Dispersion (M.A.D.) phasing to obtain the protein phase information from 32 selenomethionine sites in the MhpC asymmetric unit. The enzyme belongs to the α/β hydrolase fold family. Mechanistic studies can now be undertaken involving the analysis of the interactions of various ligands bound in at the active site.
Momordin is a ribosome inactivating protein (RIP) from the seeds of the bitter gourd, Momordica charantia. RIPs exist in two main classes. Type II RIPs, such as ricin, possess two subunits, the A- and B-chains. The A-chain is a toxin which targets ribosomes, whilst the B-chain is a lectin responsible for facilitating A-chain entry into cells. Type 1 RIPs, in contrast, are monomeric toxins, which share homology with type II RIP A-chains.
University of Southampton
Dunn, Graham Spencer
db3235ce-143a-4e6f-a674-bc3590523618
2000
Dunn, Graham Spencer
db3235ce-143a-4e6f-a674-bc3590523618
Dunn, Graham Spencer
(2000)
Crystallographic and biochemical analysis of three distinct hydrolases : Dermatophagoides pteronyssinus 1 (Der p1), momordin and the bacterial carbon-carbon hydrolase, MhpC.
University of Southampton, Doctoral Thesis.
Record type:
Thesis
(Doctoral)
Abstract
MhpC is one of six enzymes derived from the mhp operon, which collectively give rise to meta-cleavage pathway for the degradation of 3-(3-hydroxyphenyl)propionic acids (3-HPP) in Escherichia coli. These enzymes work in tandem to convert 3-HPP to metabolites which can then be fed into the Kreb's cycle for energy release. The role of MhpC in this pathway is to convert 2-hydroxy-6-ketonona-2,4-diene-1,9-dioate to 2-hydroxy-penta-2, 4-dienoate and succinate. This reaction involves the breaking of a carbon-carbon bond, which constitutes a rare catalytic event in nature. Elucidating the catalytic mechanism of MhpC will provide invaluable information at the molecular level contributing to the understanding of how biodegradation of environmental pollutants can be achieved.
The MhpC structure has been solved using Multiwavelength Anomalous Dispersion (M.A.D.) phasing to obtain the protein phase information from 32 selenomethionine sites in the MhpC asymmetric unit. The enzyme belongs to the α/β hydrolase fold family. Mechanistic studies can now be undertaken involving the analysis of the interactions of various ligands bound in at the active site.
Momordin is a ribosome inactivating protein (RIP) from the seeds of the bitter gourd, Momordica charantia. RIPs exist in two main classes. Type II RIPs, such as ricin, possess two subunits, the A- and B-chains. The A-chain is a toxin which targets ribosomes, whilst the B-chain is a lectin responsible for facilitating A-chain entry into cells. Type 1 RIPs, in contrast, are monomeric toxins, which share homology with type II RIP A-chains.
Text
770770.pdf
- Version of Record
More information
Published date: 2000
Identifiers
Local EPrints ID: 464257
URI: http://eprints.soton.ac.uk/id/eprint/464257
PURE UUID: 2439765e-e2e4-4b26-87c5-495093668891
Catalogue record
Date deposited: 04 Jul 2022 21:46
Last modified: 16 Mar 2024 19:22
Export record
Contributors
Author:
Graham Spencer Dunn
Download statistics
Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.
View more statistics