168 related articles for article (PubMed ID: 31989227)
1. Structural insight into the substrate specificity of PLP fold type IV transaminases.
Bezsudnova EY; Popov VO; Boyko KM
Appl Microbiol Biotechnol; 2020 Mar; 104(6):2343-2357. PubMed ID: 31989227
[TBL] [Abstract][Full Text] [Related]
2. Functional characterization of PLP fold type IV transaminase with a mixed type of activity from Haliangium ochraceum.
Zeifman YS; Boyko KM; Nikolaeva AY; Timofeev VI; Rakitina TV; Popov VO; Bezsudnova EY
Biochim Biophys Acta Proteins Proteom; 2019 Jun; 1867(6):575-585. PubMed ID: 30902765
[TBL] [Abstract][Full Text] [Related]
3. Biochemical and structural insights into PLP fold type IV transaminase from Thermobaculum terrenum.
Bezsudnova EY; Boyko KM; Nikolaeva AY; Zeifman YS; Rakitina TV; Suplatov DA; Popov VO
Biochimie; 2019 Mar; 158():130-138. PubMed ID: 30599183
[TBL] [Abstract][Full Text] [Related]
4. Diaminopelargonic acid transaminase from Psychrobacter cryohalolentis is active towards (S)-(-)-1-phenylethylamine, aldehydes and α-diketones.
Bezsudnova EY; Stekhanova TN; Popinako AV; Rakitina TV; Nikolaeva AY; Boyko KM; Popov VO
Appl Microbiol Biotechnol; 2018 Nov; 102(22):9621-9633. PubMed ID: 30178202
[TBL] [Abstract][Full Text] [Related]
5. Properties of Bacterial and Archaeal Branched-Chain Amino Acid Aminotransferases.
Bezsudnova EY; Boyko KM; Popov VO
Biochemistry (Mosc); 2017 Dec; 82(13):1572-1591. PubMed ID: 29523060
[TBL] [Abstract][Full Text] [Related]
6. Structural Basis of the Substrate Range and Enantioselectivity of Two (S)-Selective ω-Transaminases.
van Oosterwijk N; Willies S; Hekelaar J; Terwisscha van Scheltinga AC; Turner NJ; Dijkstra BW
Biochemistry; 2016 Aug; 55(31):4422-31. PubMed ID: 27428867
[TBL] [Abstract][Full Text] [Related]
7. Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.
Łyskowski A; Gruber C; Steinkellner G; Schürmann M; Schwab H; Gruber K; Steiner K
PLoS One; 2014; 9(1):e87350. PubMed ID: 24498081
[TBL] [Abstract][Full Text] [Related]
8. Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold.
Pavkov-Keller T; Strohmeier GA; Diepold M; Peeters W; Smeets N; Schürmann M; Gruber K; Schwab H; Steiner K
Sci Rep; 2016 Dec; 6():38183. PubMed ID: 27905516
[TBL] [Abstract][Full Text] [Related]
9. The Uncommon Active Site of D-Amino Acid Transaminase from
Bakunova AK; Nikolaeva AY; Rakitina TV; Isaikina TY; Khrenova MG; Boyko KM; Popov VO; Bezsudnova EY
Molecules; 2021 Aug; 26(16):. PubMed ID: 34443642
[TBL] [Abstract][Full Text] [Related]
10. Identification of branched-chain amino acid aminotransferases active towards (R)-(+)-1-phenylethylamine among PLP fold type IV transaminases.
Bezsudnova EY; Dibrova DV; Nikolaeva AY; Rakitina TV; Popov VO
J Biotechnol; 2018 Apr; 271():26-28. PubMed ID: 29453991
[TBL] [Abstract][Full Text] [Related]
11. Crystallographic characterization of the (R)-selective amine transaminase from Aspergillus fumigatus.
Thomsen M; Skalden L; Palm GJ; Höhne M; Bornscheuer UT; Hinrichs W
Acta Crystallogr D Biol Crystallogr; 2014 Apr; 70(Pt 4):1086-93. PubMed ID: 24699652
[TBL] [Abstract][Full Text] [Related]
12. Crystal structure and substrate specificity of the thermophilic serine:pyruvate aminotransferase from Sulfolobus solfataricus.
Sayer C; Bommer M; Isupov M; Ward J; Littlechild J
Acta Crystallogr D Biol Crystallogr; 2012 Jul; 68(Pt 7):763-72. PubMed ID: 22751661
[TBL] [Abstract][Full Text] [Related]
13. Expanding the Toolbox of R-Selective Amine Transaminases by Identification and Characterization of New Members.
Telzerow A; Paris J; Håkansson M; González-Sabín J; Ríos-Lombardía N; Gröger H; Morís F; Schürmann M; Schwab H; Steiner K
Chembiochem; 2021 Apr; 22(7):1232-1242. PubMed ID: 33242357
[TBL] [Abstract][Full Text] [Related]
14. The ω-transaminase engineering database (oTAED): A navigation tool in protein sequence and structure space.
Buß O; Buchholz PCF; Gräff M; Klausmann P; Rudat J; Pleiss J
Proteins; 2018 May; 86(5):566-580. PubMed ID: 29423963
[TBL] [Abstract][Full Text] [Related]
15. Computer Modeling Explains the Structural Reasons for the Difference in Reactivity of Amine Transaminases Regarding Prochiral Methylketones.
Teixeira IS; Farias AB; Horta BAC; Milagre HMS; de Souza ROMA; Bornscheuer UT; Milagre CDF
Int J Mol Sci; 2022 Jan; 23(2):. PubMed ID: 35054965
[TBL] [Abstract][Full Text] [Related]
16. Structure and function of branched chain aminotransferases.
Hutson S
Prog Nucleic Acid Res Mol Biol; 2001; 70():175-206. PubMed ID: 11642362
[TBL] [Abstract][Full Text] [Related]
17. Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications.
Steffen-Munsberg F; Vickers C; Kohls H; Land H; Mallin H; Nobili A; Skalden L; van den Bergh T; Joosten HJ; Berglund P; Höhne M; Bornscheuer UT
Biotechnol Adv; 2015; 33(5):566-604. PubMed ID: 25575689
[TBL] [Abstract][Full Text] [Related]
18. Structural determinants of the β-selectivity of a bacterial aminotransferase.
Wybenga GG; Crismaru CG; Janssen DB; Dijkstra BW
J Biol Chem; 2012 Aug; 287(34):28495-502. PubMed ID: 22745123
[TBL] [Abstract][Full Text] [Related]
19. Structural and biochemical characterization of the dual substrate recognition of the (R)-selective amine transaminase from Aspergillus fumigatus.
Skalden L; Thomsen M; Höhne M; Bornscheuer UT; Hinrichs W
FEBS J; 2015 Jan; 282(2):407-15. PubMed ID: 25400251
[TBL] [Abstract][Full Text] [Related]
20. Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum.
Bezsudnova EY; Nikolaeva AY; Bakunova AK; Rakitina TV; Suplatov DA; Popov VO; Boyko KM
PLoS One; 2021; 16(7):e0255098. PubMed ID: 34324538
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]