Abstract:
:The phytoene desaturase CrtI from Rubrivivax gelatinosus catalyzes simultaneously a three- and four-step desaturation producing both neurosporene and lycopene. These carotenes are intermediates for the synthesis of spheroidene and spirilloxanthin, respectively. Two different mutation libraries for the crtI gene from R. gelatinosus were constructed to screen for modified enzymes which synthesize almost exclusively either neurosporene or lycopene. The resulting mutants carried between one and four amino acid exchanges and at least one of them affected the secondary protein structure by shortening or extending one of the helices. A prominent amino acid which was exchanged in the neurosporene or lycopene-forming desaturase was leucine 208. Enzyme kinetic studies were carried out with the L208 modified desaturase and the specificities for phytoene and neurosporene as substrates determined. Higher and lower values correlate well with the higher or lower potential for the synthesis of lycopene from neurosporene. TopPred analysis of the mutations of L208 indicated that the location is in a highly hydrophobic membrane-integrated region which is a good candidate for the substrate-binding site of the desaturase.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Stickforth P,Sandmann Gdoi
10.1016/j.abb.2010.09.021subject
Has Abstractpub_date
2011-01-01 00:00:00pages
118-22issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(10)00413-3journal_volume
505pub_type
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