Amino acid sequence of anionic peroxidase from the windmill palm tree Trachycarpus fortunei.
Palm peroxidases are extremely stable and have uncommon substrate specificity. This study was designed to fill in the knowledge gap about the structures of a peroxidase from the windmill palm tree Trachycarpus fortunei. The complete amino acid sequence and partial glycosylation were determined by MALDI-top-down sequencing of native windmill palm tree peroxidase (WPTP), MALDI-TOF/TOF MS/MS of WPTP tryptic peptides, and cDNA sequencing. The propeptide of WPTP contained N- and C-terminal signal sequences which contained 21 and 17 amino acid residues, respectively. Mature WPTP was 306 amino acids in length, and its carbohydrate content ranged from 21% to 29%. Comparison to closely related royal palm tree peroxidase revealed structural features that may explain differences in their substrate specificity. The results can be used to guide engineering of WPTP and its novel applications.
Department of Molecular Biosciences and Bioengineering, University of Hawaii at Manoa , Honolulu, Hawaii 96822, United States.
Margaret R
MR
Baker
Hongwei
H
Zhao
Ivan Yu
IY
Sakharov
Qing X
QX
Li
D000595:Amino Acid Sequence; D028023:Arecaceae / Q000737:chemistry / Q000145:classification / Q000201:enzymology* / Q000235:genetics*; D001483:Base Sequence; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013379:Substrate Specificity; D014197:Trees
D010940:Plant Proteins; D010544:Peroxidases; C120494:anionic peroxidase
MALDI-TOF; amino acid sequencing; glycosylation; palm; peroxidase; top-down mass spectrometry