Crystallographic analysis of FAD-dependent glucose dehydrogenase

被引：2

作者：

Komori, Hirofumi ^{[1
,2
]}

Inaka, Koji ^{[3
]}

Furubayashi, Naoki ^{[3
]}

Honda, Michinari ^{[4
]}

Higuchi, Yoshiki ^{[2
,5
]}

机构：

[1] Kagawa Univ, Fac Educ, Takamatsu, Kagawa 7608522, Japan

[2] RIKEN, SPring Ctr 8, Mikazuki, Hyogo 6795198, Japan

[3] Maruwa Foods & Biosci Inc, Nara 6391123, Japan

[4] Ikeda Tohka Ind Co Ltd, Fukuyama, Hiroshima 7210956, Japan

[5] Univ Hyogo, Dept Life Sci, Kamigori, Hyogo 6781297, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2015年 / 71卷

基金：

日本学术振兴会;

关键词：

glucose dehydrogenase; FAD; glucose sensor; ANGSTROM RESOLUTION;

D O I：

10.1107/S2053230X15010742

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

An FAD-dependent glucose dehydrogenase (GDH) from Aspergillus terreus was purified and crystallized at 293K using the sitting-drop vapour-diffusion method. A data set was collected to a resolution of 1.6 angstrom from a single crystal at 100K using a rotating-anode X-ray source. The crystal belonged to space group P2(1), with unit-cell parameters a = 56.56, b = 135.74, c = 74.13 angstrom, = 90.37 degrees. The asymmetric unit contained two molecules of GDH. The Matthews coefficient was calculated to be 2.2 angstrom(3)Da(-1) and the solvent content was estimated to be 44%.

引用

页码：1017 / 1019

页数：3

共 50 条

[41] Commentary regarding: "Activity determination of FAD-dependent glucose dehydrogenase immobilized in PEDOT: PSS-PVA composite films for biosensor applications"
Walz, Anna-Lena
Liebl, Lana
Schmitt, Katrin
Scharfer, Philip
Schabel, Wilhelm
ENGINEERING IN LIFE SCIENCES, 2019, 19 (11): : 741 - 748
[42] Mutagenesis Study of the Cytochrome c Subunit Responsible for the Direct Electron Transfer-Type Catalytic Activity of FAD-Dependent Glucose Dehydrogenase
Yamashita, Yuki
Suzuki, Nanoha
Hirose, Nana
Kojima, Katsuhiro
Tsugawa, Wakako
Sode, Koji
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2018, 19 (04)
[43] Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells
Muhammad Nadeem Zafar
Najat Beden
Dónal Leech
Christoph Sygmund
Roland Ludwig
Lo Gorton
Analytical and Bioanalytical Chemistry, 2012, 402 : 2069 - 2077
[44] Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells
Zafar, Muhammad Nadeem
Beden, Najat
Leech, Donal
Sygmund, Christoph
Ludwig, Roland
Gorton, Lo
ANALYTICAL AND BIOANALYTICAL CHEMISTRY, 2012, 402 (06) : 2069 - 2077
[45] Designing a high-potential metal-free viologen-based redox polymer for effective wiring of FAD-dependent glucose dehydrogenase
Chandra, Shubhadeep
Lielpetere, Anna
Schuhmann, Wolfgang
SENSORS AND ACTUATORS B-CHEMICAL, 2023, 397
[46] Direct electron transfer-type bioelectrocatalysis of FAD-dependent glucose dehydrogenase using porous gold electrodes and enzymatically implanted platinum nanoclusters
Adachi, Taiki
Fujii, Takahiro
Honda, Michinari
Kitazumi, Yuki
Shirai, Osamu
Kano, Kenji
BIOELECTROCHEMISTRY, 2020, 133
[47] Bionanotechnology approach for FAD-dependent enzymes with nanomaterials sensor
Li, Ying
Chen, Shen-Ming
Yang, Cheng-Yu
Ali, M. Ajmal
AlHemaid, Fahad M. A.
SAUDI JOURNAL OF BIOLOGICAL SCIENCES, 2012, 19 (04) : 465 - 471
[48] Isolation of a FAD-GPDH gene encoding a mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase from Dunaliella salina
Yang, Wanggui
Cao, Yi
Sun, Xiaofei
Huang, Fei
He, Qinghua
Qiao, Dairong
Bai, Linhan
JOURNAL OF BASIC MICROBIOLOGY, 2007, 47 (03) : 266 - 274
[49] Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase
Tschantz, WR
Digits, JA
Pyun, HJ
Coates, RM
Casey, PJ
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (04) : 2321 - 2324
[50] Involvement of Lys-308 in the FAD-dependent oxidase activity of NADH dehydrogenase from an alkaliphilic Bacillus
Kitazume, Yayoi
Mutoh, Mamiko
Shiraki, Masato
Koyama, Noriyuki
RESEARCH IN MICROBIOLOGY, 2006, 157 (10) : 956 - 959

← 1 2 3 4 5 →