Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship.

ABSTRACT:

Background

Aldehyde-deformylating oxygenase (ADO) is a key enzyme involved in the biosynthetic pathway of fatty alk(a/e)nes in cyanobacteria. However, cADO (cyanobacterial ADO) showed extreme low activity with the k _cat value below 1 min^-1, which would limit its application in biofuel production. To identify the activity related key residues of cADO is urgently required.

Results

The amino acid residues which might affect cADO activity were identified based on the crystal structures and sequence alignment of cADOs, including the residues close to the di-iron center (Tyr39, Arg62, Gln110, Tyr122, Asp143 of cADO-1593), the protein surface (Trp 178 of cADO-1593), and those involved in two important hydrogen bonds (Gln49, Asn123 of cADO-1593, and Asp49, Asn1

SUBMITTER: Wang Q 

PROVIDER: S-EPMC5356278 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature