Turning a monocovalent flavoprotein into a bicovalent flavoprotein by structure-inspired mutagenesis

Malgorzata Kopacz, Marco W Fraaije

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Abstrakt

A recently discovered class of bicovalent flavoproteins is an interesting group of
enzymes because of their unusual cofactor binding mode, their open active sites and the
bulky substrates they can accept. Through a sequence comparison study we have identified
a conserved sequence region in bicovalent flavoproteins that is different from monocovalent
flavoproteins. Based on this and the available structural information we have designed
mutants of the prototype monocovalent flavoprotein, 6-hydroxy-d-nicotine oxidase (6HDNO),
in order to introduce a second cofactor-protein linkage. Two amino acid replacements,
namely histidine 130 to a cysteine and leucine 138 to a histidine, were sufficient to create a
bicovalent 6HDNO. The introduced cysteine forms a covalent bond with FAD as found in
natural bicovalent flavoproteins, while the second mutation was found to be essential to …
OriginalsprogEngelsk
TidsskriftBioorganic & Medicinal Chemistry
Vol/bind22
Udgave nummer20
Sider (fra-til)5621-5627
ISSN0968-0896
DOI
StatusUdgivet - 2014
Udgivet eksterntJa

Fingeraftryk

Dyk ned i forskningsemnerne om 'Turning a monocovalent flavoprotein into a bicovalent flavoprotein by structure-inspired mutagenesis'. Sammen danner de et unikt fingeraftryk.

Citationsformater