Biochemical characterisation of DMSP Lyases in Marine Bacteria and Phytoplankton

Newton-Payne, Simone (2015) Biochemical characterisation of DMSP Lyases in Marine Bacteria and Phytoplankton. Doctoral thesis, University of East Anglia.

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Abstract

Dimethylsulphoniopropionate (DMSP) is the most abundant sulphur molecule in
the oceans. Catabolism of DMSP by marine organisms is important both for the
global movement of sulphur and as a carbon and sulphur source for microbial life.
The molecular basis of DMSP catabolism had been revealed by the discovery of a
DMSP demethylase and six different lyases in marine bacteria. However, at the
start of this study in 2009 no eukaryotic DMSP lyase had been isolated, purified or
characterized from axenic cultures, and there was little information on the
enzymology of any of the bacterial DMSP lyase enzymes. The work presented in
this thesis identifies the requirement of the three bacterial cupin DMSP lyases
DddL, DddQ and DddW for metal cofactors, and also establishes the enzymology
and biochemistry of these cupin-containing DMSP lyases. The presence of a
typical DMSP lyase in the coccolithophore Emiliania huxleyi RCC1217 is also
demonstrated for the first time from bacteria-free cultures by application of
previously successful techniques used in the purification of bacterial ddd genes.
Combined these findings provide new insights into the mechanisms of cleavage of
DMSP by bacteria and phytoplankton and expand our understanding of the
enzyme diversity involved in this process.

Item Type:	Thesis (Doctoral)
Faculty \ School:	Faculty of Science > School of Biological Sciences
Depositing User:	Stacey Armes
Date Deposited:	28 Jun 2016 16:10
Last Modified:	01 Oct 2018 00:38
URI:	https://ueaeprints.uea.ac.uk/id/eprint/59619
DOI:

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