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1. Thermostabilizing ketoreductase ChKRED20 by consensus mutagenesis at dimeric interfaces

Author:
Zhong-Liu Wu,   et al.   ; Yu-Jie Yang; Xiao-Qiong Pei; Yan Liu;     Show all 4 Authors
Source:
Enzyme and microbial technology 2022 v.158 pp. 110052
ISSN:
0141-0229
Subject:
catalytic activity; enzymes; half life; mutagenesis; mutants; simulation models; technology; temperature; thermal stability
Abstract:
... Protein stability is crucial in enzymatic catalysis. To improve the efficiency in the searching for thermostablizing mutations, we applied a sequence consensus approach focusing on dimeric interface residues of ketoreductase ChKRED20. The strategy returned a success rate of 43%, revealing 9 beneficial mutations from 21 candidates with improved kinetic or thermodynamic stability. Several combinator ...
DOI:
10.1016/j.enzmictec.2022.110052

2. Enhancing the thermal stability of ketoreductase ChKRED12 using the FireProt web server

Author:
Zhong-Liu Wu,   et al.   ; Yan Liu; Zi-Yi Li; Chao Guo; Can Cui; Hui Lin;     Show all 6 Authors
Source:
Process biochemistry 2021 v.101 pp. 207-212
ISSN:
1359-5113
Subject:
Internet; amino acids; chromatography; enzymes; half life; mutants; space and time; temperature; thermal stability
Abstract:
... Ketoreductase ChKRED12 catalyzes the asymmetric bioreduction of ethyl 3-oxo-3-(2-thienyl) propanoate to produce the key chiral intermediate of duloxetine. To improve the robustness of the enzyme, we used the FireProt web server to predict potential thermostabilizing amino acid substitutions, and we experimentally confirmed 4 beneficial substitutions (S79P, L128M, V162I and G163A). These substituti ...
DOI:
10.1016/j.procbio.2020.11.018

3. Asymmetric Epoxidation and Sulfoxidation Catalyzed by a New Styrene Monooxygenase from Bradyrhizobium

Author:
Zhong-Liu Wu,   et al.   ; Can Cui; Hui Lin; Wei Pu; Chao Guo; Yan Liu; Xiao-Qiong Pei;     Show all 7 Authors
Source:
Applied biochemistry and biotechnology 2021 v.193 no.1 pp. 65-78
ISSN:
0273-2289
Subject:
Bradyrhizobium; Soil Moisture and Ocean Salinity satellite; amino acids; biotechnology; databases; enantiomers; epoxidation reactions; oxidoreductases; styrene
Abstract:
... Asymmetric epoxidation catalyzed with styrene monooxygenase (SMO) is a powerful enzymatic process producing enantiopure styrene epoxide derivatives. To establish a more diversified reservoir of SMOs, a new SMO from Bradyrhizobium sp. ORS 375, named BrSMO, was mined from the database and characterized. BrSMO was constituted of an epoxygenase component of 415 amino acid residues and an NADH-dependen ...
DOI:
10.1007/s12010-020-03413-8

4. Characterization of two styrene monooxygenases from marine microbes

Author:
Zhong-Liu Wu,   et al.   ; Wei Pu; Can Cui; Chao Guo;     Show all 4 Authors
Source:
Enzyme and microbial technology 2018 v.112 pp. 29-34
ISSN:
0141-0229
Subject:
Escherichia coli; Marinobacterium; Pseudomonas; alcohols; biocatalysts; epoxidation reactions; epoxides; genome; microorganisms; nitrogen dioxide; oxygenases; pH; stereoselectivity; styrene
Abstract:
... Styrene monooxygenases (SMOs) are highly stereoselective enzymes that catalyze the formation of chiral epoxides as versatile building blocks. To expand the enzyme toolbox, two bacterial SMOs were identified from the genome of marine microbes Paraglaciecola agarilytica NO2 and Marinobacterium litorale DSM 23545, and heterologously expressed in Escherichia coli in soluble form. Both of the resulting ...
DOI:
10.1016/j.enzmictec.2018.02.001

5. Construction and functional analysis of a whole-cell biocatalyst based on CYP108N7

Author:
Zhong-Liu Wu,   et al.   ; Chao Guo;     Show all 2 Author
Source:
Enzyme and Microbial Technology 2017 pp. -
ISSN:
0141-0229
Subject:
Escherichia coli; NADP (coenzyme); Rhodococcus wratislaviensis; biocatalysts; biotechnology; cytochrome P-450; dehalogenation; electron transfer; enzymes; genome; glucose; hydroxylation; spinach; stereochemistry
Abstract:
... Cytochrome P450 enzymes are versatile biocatalysts with great potential in biotechnology. A new bacterial P450 was identified from the genome of Rhodococcus wratislaviensis NBRC 100605 and annotated as CYP108N7. The enzyme accepted the ferredoxin and ferredoxin reductase from spinach as surrogate redox partners for improved electron transfer efficiency. It was heterologous expressed in Escherichia ...
DOI:
10.1016/j.enzmictec.2017.06.016

6. Functional characterization of an (R)-selective styrene monooxygenase from streptomyces sp. NRRL S-31

Author:
Zhong-Liu Wu,   et al.   ; Can Cui; Chao Guo; Hui Lin; Zhao-Yun Ding; Yan Liu;     Show all 6 Authors
Source:
Enzyme and microbial technology 2019 pp. -
ISSN:
0141-0229
Subject:
Soil Moisture and Ocean Salinity satellite; Streptomyces; alkenes; epoxidation reactions; genome; oxidoreductases; plasmids; stereoselectivity; styrene
Abstract:
... Styrene monooxygenases (SMOs) are two-component enzymes known to catalyze the epoxidation of styrene to (S)-styrene oxide. In this work, we identified a new oxygenase component, named StStyA, from the genome of Streptomyces sp. NRRL S-31. StStyA displayed complementary stereoselectivity to all of the known SMOs when coupled with a known reductase component (PsStyB), which made it the first natural ...
DOI:
10.1016/j.enzmictec.2019.109391

7. Switchable asymmetric bio-epoxidation of α,β-unsaturated ketones

Author:
Zhong-Liu Wu,   et al.   ; Yu-Chang Liu;     Show all 2 Author
Source:
Chemical communications 2016 v.52 no.6 pp. 1158-1161
ISSN:
1364-548X
Subject:
chemical reactions; epoxides; ketones
Abstract:
... Efficient asymmetric bio-epoxidation of electron-deficient α,β-unsaturated ketones was realized via a tandem reduction-epoxidation-dehydrogenation cascade, which proceeds in a switchable manner to afford either chiral epoxy ketones or allylic epoxy alcohols with up to >99% yield and >99%ee. ...
DOI:
10.1039/c5cc07548c

8. Stereo-complementary bioreduction of saturated N-heterocyclic ketones

Author:
Zhong-Liu Wu,   et al.   ; Chao Li; Yan Liu; Xiao-Qiong Pei;     Show all 4 Authors
Source:
Process biochemistry 2017 v.56 pp. 90-97
ISSN:
1359-5113
Subject:
enantiomers; isopropyl alcohol; ketones; reducing agents; stereochemistry
Abstract:
... The asymmetric bioreduction of several saturated N-heterocyclic ketones is demonstrated in a stereo-complementary fashion using the ketoreductases READH and ChKRED20 for the production of (S)- and (R)-alcohols, respectively. The reaction accepts substrates with a five-, six- or seven-membered ring, and exhibits excellent stereoselectivity when using 2-propanol as both the ultimate reducing agent a ...
DOI:
10.1016/j.procbio.2017.03.002

9. Rapid asymmetric reduction of ethyl 4-chloro-3-oxobutanoate using a thermostabilized mutant of ketoreductase ChKRED20

Author:
Zhong-Liu Wu,   et al.   ; Feng-Jiao Zhao; Xiao-Qiong Pei; Zhi-Qiang Ren;     Show all 4 Authors
Source:
Applied microbiology and biotechnology 2016 v.100 no.8 pp. 3567-3575
ISSN:
0175-7598
Subject:
Chryseobacterium; catalysts; drugs; enantiomers; half life; mutants; mutation; polymerase chain reaction; screening; stereochemistry; temperature; thermal stability
Abstract:
... Ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE) is an important chiral intermediate for the synthesis of “blockbuster” drug statins. The carbonyl reductase ChKRED20 from Chryseobacterium sp. CA49 was found to catalyze the bio-reductive production of (S)-CHBE with excellent stereoselectivity (>99.5 % ee). Perceiving a capacity for improvement, we sought to increase the thermostability of ChKRED20 ...
DOI:
10.1007/s00253-015-7200-2

10. Efficient bioreductive production of (S)-N-Boc-3-hydroxypiperidine using ketoreductase ChKRED03

Author:
Zhong-Liu Wu,   et al.   ; Guang-Peng Xu; Hai-Bo Wang;     Show all 3 Authors
Source:
Process biochemistry 2016 v.51 no.7 pp. 881-885
ISSN:
1359-5113
Subject:
B-lymphocytes; Chryseobacterium; NADP (coenzyme); alcohols; antineoplastic agents; buffers; catalysts; enzyme activity; genome; industrial applications; inventories; pH; potassium phosphates; screening
Abstract:
... Ibrutinib is an anticancer drug targeting B-cell malignancies. The key chiral intermediate for ibrutinib synthesis is the alcohol (S)-N-Boc-3-hydroxypiperidine ((S)-NBHP), which can be produced via ketoreductase (KRED)-catalyzed bioreduction. After screening a small inventory of 27 KREDs mined from the genome of Chryseobacterium sp. CA49, ChKRED03 was selected as the best performer, leading to the ...
DOI:
10.1016/j.procbio.2016.04.008

11. Two “classical” Old Yellow Enzymes from Chryseobacterium sp. CA49: Broad substrate specificity of Chr-OYE1 and limited activity of Chr-OYE2

Author:
Zhong-Liu Wu,   et al.   ; Xiao-Qiong Pei; Meng-Yu Xu;     Show all 3 Authors
Source:
Journal of molecular catalysis 2016 v.123 pp. 91-99
ISSN:
1381-1177
Subject:
Agrobacterium radiobacter; Chryseobacterium; Escherichia coli; Shewanella oneidensis; catalytic activity; enzymes; genome; stereochemistry; substrate specificity; tyrosine
Abstract:
... Two putative Old Yellow Enzyme (OYE) homologues, Chr-OYE1 and Chr-OYE2, were identified from the genome of Chryseobacterium sp. CA49 as new members of the “classical” subfamily. Chr-OYE1 and Chr-OYE2 were most closely related to the SYE4 from Shewanella oneidensis and NerA from Agrobacterium radiobacter with 41% and 45% identity, respectively. Both enzymes were expressed in Escherichia coli in sol ...
DOI:
10.1016/j.molcatb.2015.11.008

12. Structure-guided engineering of ChKRED20 from Chryseobacterium sp. CA49 for asymmetric reduction of aryl ketoesters

Author:
Zhong-Liu Wu,   et al.   ; Tong-Biao Li; Feng-Jiao Zhao; Zhongchuan Liu; Yun Jin; Yan Liu; Xiao-Qiong Pei; Zhi-Gang Zhang; Ganggang Wang;     Show all 9 Authors
Source:
Enzyme and microbial technology 2019 v.125 pp. 29-36
ISSN:
0141-0229
Subject:
Chryseobacterium; amino acids; aromatic compounds; catalytic activity; crystal structure; engineering; enzymes; genome; industrial applications; isopropyl alcohol; ketones; mutagenesis; mutants; reducing agents
Abstract:
... ChKRED20 is a robust NADH-dependent ketoreductase identified from the genome of Chryseobacterium sp. CA49 that can use 2-propanol as the ultimate reducing agent. The wild-type can reduce over 100 g/l ketones for some pharmaceutical relevant substrates, exhibiting a remarkable potential for industrial application. In this work, to overcome the limitation of ChKRED20 to aryl ketoesters, we first ref ...
DOI:
10.1016/j.enzmictec.2019.03.001

13. Single mutations of ketoreductase ChKRED20 enhance the bioreductive production of (1S)-2-chloro-1-(3, 4-difluorophenyl) ethanol

Author:
Zhong-Liu Wu,   et al.   ; Feng-Jiao Zhao; Yan Liu; Xiao-Qiong Pei; Chao Guo;     Show all 5 Authors
Source:
Applied microbiology and biotechnology 2017 v.101 no.5 pp. 1945-1952
ISSN:
0175-7598
Subject:
Chryseobacterium; amino acid substitution; drugs; enantiomers; half life; inventories; mutagenesis; mutants; polymerase chain reaction; screening; stereochemistry
Abstract:
... (1S)-2-chloro-1-(3, 4-difluorophenyl) ethanol ((S)-CFPL) is an intermediate for the drug ticagrelor, and is manufactured via chemical approaches. To develop a biocatalytic solution to (S)-CFPL, an inventory of ketoreductases from Chryseobacterium sp. CA49 were rescreened, and ChKRED20 was found to catalyze the reduction of the ketone precursor with excellent stereoselectivity (>99 % ee). After scr ...
DOI:
10.1007/s00253-016-7947-0

14. Characterization of a robust anti-Prelog short-chain dehydrogenase/reductase ChKRED20 from Chryseobacterium sp. CA49

Author:
Zhong-Liu Wu,   et al.   ; Tuo-Xian Tang; Yan Liu;     Show all 3 Authors
Source:
Journal of Molecular Catalysis. B, Enzymatic 2014 v.105 pp. 82-88
ISSN:
1381-1177
Subject:
Chryseobacterium; additives; alcohols; catalytic activity; detergents; enzyme activity; half life; heat inactivation; metal ions; pH; solvents; stereochemistry; temperature
Abstract:
... ChKRED20 is a short-chain dehydrogenase/reductase (SDR) cloned from Chryseobacterium sp. CA49 for the anti-Prelog bioreduction of 3,5-bis(trifluoromethyl)acetophenone to produce the chiral alcohol intermediate for aprepitant. Purified ChKRED20 showed broad pH adaptability and stability with 91% of the maximal activity retained at pH 10.0. The temperature dependence of activity reached the maxima a ...
DOI:
10.1016/j.molcatb.2014.03.020

15. An enoate reductase Achr-OYE4 from Achromobacter sp. JA81: characterization and application in asymmetric bioreduction of C=C bonds

Author:
Zhong-Liu Wu,   et al.   ; Hai-Bo Wang; Xiao-Qiong Pei;     Show all 3 Authors
Source:
Applied microbiology and biotechnology 2014 v.98 no.2 pp. 705-715
ISSN:
0175-7598
Subject:
Achromobacter; Escherichia coli; NAD (coenzyme); NADP (coenzyme); alkenes; genome; glucose; sequence analysis; spectral analysis
Abstract:
... A putative enoate reductase, Achr-OYE4, was mined from the genome of Achromobacter sp. JA81, expressed in Escherichia coli, and was characterized. Sequence analysis and spectral properties indicated that Achr-OYE4 is a typical flavin mononucleotide-dependent protein; it preferred NADH over NADPH as a cofactor. The heterologously expressed protein displayed good activity and excellent stereoselecti ...
DOI:
10.1007/s00253-013-4899-5
PubMed:
23644746

16. Identification and characterization of a novel “thermophilic-like” Old Yellow Enzyme from the genome of Chryseobacterium sp. CA49

Author:
Zhong-Liu Wu,   et al.   ; Meng-Yu Xu; Xiao-Qiong Pei;     Show all 3 Authors
Source:
Journal of Molecular Catalysis. B, Enzymatic 2014 v.108 pp. 64-71
ISSN:
1381-1177
Subject:
Bacillus subtilis; Chryseobacterium; alkenes; biocatalysis; dimethyl sulfoxide; ethylene glycol; genome; half life; heat inactivation; heat tolerance; solvents
Abstract:
... A putative Old Yellow Enzyme (OYE) homologue, Chr-OYE3, was identified from the genome of Chryseobacterium sp. CA49 as a new member of the “thermophilic-like” OYE subfamily. Chr-OYE3 is most closely related to YqjM from Bacillus subtilis with 51% identity. The heterologously expressed enzyme adopted two oligomeric states in solutions, dimers and tetramers. It can reduce a spectrum of activated alk ...
DOI:
10.1016/j.molcatb.2014.07.002

17. Improving the thermostability of feruloyl esterase by DNA shuffling and site-directed mutagenesis

Author:
Zhong-Liu Wu,   et al.   ; Jing-Jing Li; Xiao-Qiong Pei; Shuai-Bing Zhang;     Show all 4 Authors
Source:
Process Biochemistry 2015 v.50 pp. 1783-1787
ISSN:
1359-5113
Subject:
DNA shuffling; corn stover; ferulic acid; feruloyl esterase; fungi; half life; site-directed mutagenesis; thermal stability
Abstract:
... Feruloyl esterases (FAE) with high thermostability are greatly desired for efficient and economical industrial processes. A DNA shuffling strategy was applied to generate a chimeric library from four homologous FAEs originated from fungi. Chimeras with enhanced thermal stability compared to the parental FAEs were identified, which contained segments from 3 or 4 of the parental enzymes. After furth ...
DOI:
10.1016/j.procbio.2015.08.009

18. Crystal structure and iterative saturation mutagenesis of ChKRED20 for expanded catalytic scope

Author:
Zhong-Liu Wu,   et al.   ; Feng-Jiao Zhao; Yun Jin; Zhongchuan Liu; Chao Guo; Tong-Biao Li; Zi-Yi Li; Ganggang Wang;     Show all 8 Authors
Source:
Applied microbiology and biotechnology 2017 v.101 no.23-24 pp. 8395-8404
ISSN:
0175-7598
Subject:
alanine; alcohols; crystal structure; ketones; molecular models; mutagenesis; mutants; stereoselectivity
Abstract:
... ChKRED20 is an efficient and robust anti-Prelog ketoreductase that can catalyze the reduction of ketones to chiral alcohols as pharmaceutical intermediates with great industrial potential. To overcome its limitation on the bioreduction of ortho-substituted acetophenone derivatives, the X-ray crystal structure of the apo-enzyme of ChKRED20 was determined at a resolution of 1.85 Å and applied to the ...
DOI:
10.1007/s00253-017-8556-2

19. Identification of amino acid residues responsible for increased thermostability of feruloyl esterase A from Aspergillus niger using the PoPMuSiC algorithm

Author:
Zhong-Liu Wu,   et al.   ; Shuai-Bing Zhang;     Show all 2 Author
Source:
Bioresource technology 2011 v.102 no.2 pp. 2093-2096
ISSN:
0960-8524
Subject:
thermal stability; Aspergillus niger; energy; Komagataella pastoris; esterases; amino acid substitution; amino acids; hydrolysis; site-directed mutagenesis; algorithms; half life
Abstract:
... Feruloyl esterases are key enzymes involved in the complete hydrolysis of hemicellulose. In order to improve the thermostability of feruloyl esterase A (FaeA) from Aspergillus niger CIB 423.1, the PoPMuSiC algorithm was applied to predict the folding free energy change (ΔΔG) of amino acid substitutions. Four amino acid substitutions (S92A, D93G, D174A and S187F) were introduced into the enzyme by ...
DOI:
10.1016/j.biortech.2010.08.019
PubMed:
20801026

20. Bioreductive production of enantiopure (S)-duloxetine intermediates catalyzed with ketoreductase ChKRED15

Author:
Zhong-Liu Wu,   et al.   ; Zhi-Qiang Ren; Yan Liu; Xiao-Qiong Pei; Hai-Bo Wang;     Show all 5 Authors
Source:
Journal of molecular catalysis 2015 v.113 pp. 76-81
ISSN:
1381-1177
Subject:
alcohols; antidepressants; catalytic activity; enantiomers; mutants; mutation; recycling; sequence alignment; stereochemistry
Abstract:
... The blockbuster antidepressant drug duloxetine contains one stereo-center derived from chiral alcohol intermediates. The stereoselective bioreductive production of five of such intermediates could be achieved using the recombinant ketoreductase ChKRED15, yielding the enantiopure (S)-alcohols with >99% ee. Sequence alignment indicated that ChKRED15 lacks the conserved G-rich motif, which was then a ...
DOI:
10.1016/j.molcatb.2015.01.008