Identification of branched-chain amino acid aminotransferases active towards (R)-(+)-1-phenylethylamine among PLP fold type IV transaminases

被引:13
作者
Bezsudnova, Ekaterina Yu. [1 ]
Dibrova, Daria V. [2 ]
Nikolaeva, Alena Yu. [1 ,3 ]
Rakitina, Tatiana V. [1 ,3 ]
Popov, Vladimir O. [1 ,3 ]
机构
[1] Russian Acad Sci, Bach Inst Biochem, Biotechnol Res Ctr, Leninsky Ave 33,Bldg 2, Moscow 119071, Russia
[2] Lomonosov Moscow State Univ, Belozersky Inst Physicochem Biol, Leninskie Gory 1-73, Moscow 119991, Russia
[3] Natl Res Ctr, Kurchatov Inst, Kurchatov Complex NBICS Technol, Akad Kurchatova Sq 1, Moscow 123182, Russia
基金
俄罗斯科学基金会;
关键词
Branched-chain amino acid aminotransferases; (R)-selectivity; (R)-(+)-1-phenylethylamine; Bioinformatics analysis; PURIFICATION; PROTEIN;
D O I
10.1016/j.jbiotec.2018.02.005
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
New class IV transaminases with activity towards L-Leu, which is typical of branched-chain amino acid aminotransferases (BCAT), and with activity towards (R)-(+)-1-phenylethylamine ((R)-PEA), which is typical of (R)selective (R)-amine: pyruvate transaminases, were identified by bioinformatics analysis, obtained in recombinant form, and analyzed. The values of catalytic activities in the reaction with L-Leu and (R)-PEA are comparable to those measured for characteristic transaminases with the corresponding specificity. Earlier, (R)-selective class IV transaminases were found to be active, apart from (R)-PEA, only with some other (R)-primary amines and D-amino acids. Sequences encoding new transaminases with mixed type of activity were found by searching for changes in the conserved motifs of sequences of BCAT by different bioinformatics tools.
引用
收藏
页码:26 / 28
页数:3
相关论文
共 17 条
[1]  
[Anonymous], ARCH BIOCHEM BIOPHYS
[2]   Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein from Spiroplasma melliferum KC3 [J].
Boyko, Konstantin ;
Gorbacheva, Marina ;
Rakitina, Tatiana ;
Korzhenevskiy, Dmitry ;
Vanyushkina, Anna ;
Kamashev, Dmitry ;
Lipkin, Alexey ;
Popov, Vladimir .
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2015, 71 :24-27
[3]   First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines [J].
Boyko, Konstantin M. ;
Stekhanova, Tatiana N. ;
Nikolaeva, Alena Yu ;
Mardanov, Andrey V. ;
Rakitin, Andrey L. ;
Ravin, Nikolai V. ;
Bezsudnova, Ekaterina Yu ;
Popov, Vladimir O. .
EXTREMOPHILES, 2016, 20 (02) :215-225
[4]   NONIDENTITY OF ASPARTATE AND AROMATIC AMINOTRANSFERASE COMPONENTS OF TRANSAMINASE-A IN ESCHERICHIA-COLI [J].
COLLIER, RH ;
KOHLHAW, G .
JOURNAL OF BACTERIOLOGY, 1972, 112 (01) :365-&
[5]   Expanded microbial genome coverage and improved protein family annotation in the COG database [J].
Galperin, Michael Y. ;
Makarova, Kira S. ;
Wolf, Yuri I. ;
Koonin, Eugene V. .
NUCLEIC ACIDS RESEARCH, 2015, 43 (D1) :D261-D269
[6]   Rational assignment of key motifs for function guides in silico enzyme identification [J].
Hoehne, Matthias ;
Schaetzle, Sebastian ;
Jochens, Helge ;
Robins, Karen ;
Bornscheuer, Uwe T. .
NATURE CHEMICAL BIOLOGY, 2010, 6 (11) :807-813
[7]   A novel transaminase, (R)-amine:pyruvate aminotransferase, from Arthrobacter sp. KNK168 (FERM BP-5228): purification, characterization, and gene cloning [J].
Iwasaki, Akira ;
Matsumoto, Keiji ;
Hasegawa, Junzo ;
Yasohara, Yoshihiko .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2012, 93 (04) :1563-1573
[8]   Characterization of (R)-selective amine transaminases identified by in silico motif sequence blast [J].
Jiang, Jinju ;
Chen, Xi ;
Zhang, Dalong ;
Wu, Qiaqing ;
Zhu, Dunming .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2015, 99 (06) :2613-2621
[9]   Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold [J].
Pavkov-Keller, Tea ;
Strohmeier, Gernot A. ;
Diepold, Matthias ;
Peeters, Wilco ;
Smeets, Natascha ;
Schuermann, Martin ;
Gruber, Karl ;
Schwab, Helmut ;
Steiner, Kerstin .
SCIENTIFIC REPORTS, 2016, 6
[10]   Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase [J].
Peisach, D ;
Chipman, DM ;
Van Ophem, PW ;
Manning, JM ;
Ringe, D .
BIOCHEMISTRY, 1998, 37 (14) :4958-4967