Crystallization and preliminary crystallographic analysis of two eukaryotic fructosyl peptide oxidases

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 69; no. 2; pp. 130 - 133
• Main Authors: Ichiyanagi, Atsushi, Hirokawa, Kozo, Gomi, Keiko, Nakatsu, Toru, Kato, Hiroaki, Kajiyama, Naoki
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.02.2013
• Subjects: Amino Acid Oxidoreductases - chemistry; Catalysis; Coniochaeta sp; Crystallization; Crystallization Communications; Crystallography; Crystallography, X-Ray; Crystals; Diagnosis; diagnosis of diabetes; Diffraction; Electrophoresis, Polyacrylamide Gel; Eupenicillium - enzymology; Eupenicillium terrenum; Eurotiales - enzymology; fructosyl peptide oxidase; haemoglobin A1c; Oxidase; Peptides; Eupenicillium terrenum; Coniochaeta sp; haemoglobin A1c; fructosyl peptide oxidase; diagnosis of diabetes
• DOI: 10.1107/S1744309112051445
• ISSN: 1744-3091

Fructosyl peptide oxidase (FPOX) catalyses the oxidation of α‐glycated dipeptides such as Nα‐(1‐deoxy‐D‐fructos‐1‐yl)‐L‐valyl‐L‐histidine (Fru‐ValHis) and is used in the diagnosis of diabetes mellitus. Here, two thermostable mutants of FPOX, CFP‐T7 and EFP‐T5M, were crystallized by the sitting‐drop vapour‐diffusion method. The crystal of CFP‐T7 belonged to the tetragonal space group P41212, with unit‐cell parameters a = b = 110.09, c = 220.48 Å, and that of EFP‐T5M belonged to the monoclinic space group P21, with unit‐cell parameters a = 43.00, b = 230.05, c = 47.27 Å, β = 116.99°. The crystals of CFP‐T7 and EFP‐T5M diffracted to 1.8 and 1.6 Å resolution, respectively.