181 related articles for article (PubMed ID: 38003383)
1. Expanded Substrate Specificity in D-Amino Acid Transaminases: A Case Study of Transaminase from
Shilova SA; Matyuta IO; Petrova ES; Nikolaeva AY; Rakitina TV; Minyaev ME; Boyko KM; Popov VO; Bezsudnova EY
Int J Mol Sci; 2023 Nov; 24(22):. PubMed ID: 38003383
[TBL] [Abstract][Full Text] [Related]
2. To the Understanding of Catalysis by D-Amino Acid Transaminases: A Case Study of the Enzyme from
Shilova SA; Khrenova MG; Matyuta IO; Nikolaeva AY; Rakitina TV; Klyachko NL; Minyaev ME; Boyko KM; Popov VO; Bezsudnova EY
Molecules; 2023 Feb; 28(5):. PubMed ID: 36903355
[TBL] [Abstract][Full Text] [Related]
3. In search for structural targets for engineering d-amino acid transaminase: modulation of pH optimum and substrate specificity.
Shilova SA; Matyuta IO; Khrenova MG; Nikolaeva AY; Klyachko NL; Minyaev ME; Khomutov AR; Boyko KM; Popov VO; Bezsudnova EY
Biochem J; 2023 Aug; 480(16):1267-1284. PubMed ID: 37548495
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. Multifunctionality of arginine residues in the active sites of non-canonical d-amino acid transaminases.
Bakunova AK; Matyuta IO; Minyaev ME; Isaikina TY; Boyko KM; Popov VO; Bezsudnova EY
Arch Biochem Biophys; 2024 Jun; 756():110011. PubMed ID: 38649133
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. 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]
8. 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]
9. Bacillus anthracis ω-amino acid:pyruvate transaminase employs a different mechanism for dual substrate recognition than other amine transaminases.
Steffen-Munsberg F; Matzel P; Sowa MA; Berglund P; Bornscheuer UT; Höhne M
Appl Microbiol Biotechnol; 2016 May; 100(10):4511-21. PubMed ID: 26795966
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. Active site model of (R)-selective ω-transaminase and its application to the production of D-amino acids.
Park ES; Dong JY; Shin JS
Appl Microbiol Biotechnol; 2014 Jan; 98(2):651-60. PubMed ID: 23576035
[TBL] [Abstract][Full Text] [Related]
12. Creation of (
Voss M; Xiang C; Esque J; Nobili A; Menke MJ; André I; Höhne M; Bornscheuer UT
ACS Chem Biol; 2020 Feb; 15(2):416-424. PubMed ID: 31990173
[TBL] [Abstract][Full Text] [Related]
13. 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]
14. 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]
15. The substrate specificity, enantioselectivity and structure of the (R)-selective amine : pyruvate transaminase from Nectria haematococca.
Sayer C; Martinez-Torres RJ; Richter N; Isupov MN; Hailes HC; Littlechild JA; Ward JM
FEBS J; 2014 May; 281(9):2240-53. PubMed ID: 24618038
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. In vivo plug-and-play: a modular multi-enzyme single-cell catalyst for the asymmetric amination of ketoacids and ketones.
Farnberger JE; Lorenz E; Richter N; Wendisch VF; Kroutil W
Microb Cell Fact; 2017 Jul; 16(1):132. PubMed ID: 28754115
[TBL] [Abstract][Full Text] [Related]
18. On the flexibility of the cellular amination network in
Schulz-Mirbach H; Müller A; Wu T; Pfister P; Aslan S; Schada von Borzyskowski L; Erb TJ; Bar-Even A; Lindner SN
Elife; 2022 Jul; 11():. PubMed ID: 35876664
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. Role reversal for substrates and inhibitors. Slow inactivation of D-amino acid transaminase by its normal substrates and protection by inhibitors.
Bhatia MB; Martinez del Pozo A; Ringe D; Yoshimura T; Soda K; Manning JM
J Biol Chem; 1993 Aug; 268(24):17687-94. PubMed ID: 8349653
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]