Eric J. Yik

ORCID: 0000-0003-0204-531X
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Advanced biosensing and bioanalysis techniques
  • Enzyme Production and Characterization
  • Microbial Metabolites in Food Biotechnology
  • DNA and Nucleic Acid Chemistry
  • CRISPR and Genetic Engineering
  • Enzyme Catalysis and Immobilization
  • Microbial Natural Products and Biosynthesis
  • Biofuel production and bioconversion
  • Microbial Metabolic Engineering and Bioproduction
  • X-ray Diffraction in Crystallography
  • Advanced Proteomics Techniques and Applications
  • Innovative Microfluidic and Catalytic Techniques Innovation
  • Genomics and Phylogenetic Studies
  • Crystallization and Solubility Studies
  • RNA and protein synthesis mechanisms
  • RNA Interference and Gene Delivery
  • Natural Antidiabetic Agents Studies
  • Chemical Synthesis and Analysis
  • Biochemical and Molecular Research
  • Biosensors and Analytical Detection
  • Bacterial Genetics and Biotechnology
  • Bacteriophages and microbial interactions
  • Microbial metabolism and enzyme function

University of California, Irvine
2019-2023

California State University, Fullerton
2013-2017

Most DNA polymerase libraries sample unknown portions of mutational space and are constrained by the limitations random mutagenesis. Here we describe a programmed allelic mutagenesis (PAM) strategy to comprehensively evaluate all possible single-point mutations in entire catalytic domain replicative polymerase. By applying PAM with ultrafast high-throughput screening, show how polymerases can be mapped for that exhibit enhanced activity unnatural nucleic acid substrates. We suggest...

10.1021/acssynbio.0c00236 article EN ACS Synthetic Biology 2020-06-12

Synthetic genetic polymers (xeno-nucleic acids, XNAs) have the potential to transition aptamers from laboratory tools therapeutic agents, but additional functionality is needed compete with antibodies. Here, we describe evolution of a biologically stable artificial system composed α-l-threofuranosyl nucleic acid (TNA) that facilitates production backbone- and base-modified termed "threomers" function as high quality protein capture reagents. Threomers were discovered against two prototypical...

10.1021/acssynbio.1c00481 article EN cc-by-nc-nd ACS Synthetic Biology 2021-11-05

Natural and modified nucleoside triphosphates impact nearly every major aspect of healthcare research from DNA sequencing to drug discovery. However, a scalable synthetic route these molecules has long been hindered by the need for purification high performance liquid chromatography (HPLC). Here, we describe fundamentally different approach that uses novel P(V) pyrene pyrophosphate reagent generate derivatives are purified silica gel converted desired compounds on scales vastly exceeding...

10.1021/jacs.9b04728 article EN Journal of the American Chemical Society 2019-07-12

Artificial genetic polymers (XNAs) have enormous potential as new materials for synthetic biology, biotechnology, and molecular medicine; yet, very little is known about the biochemical properties of XNA polymerases that been developed to synthesize reverse-transcribe polymers. Here, we compare substrate specificity, thermal stability, reverse transcriptase activity, fidelity laboratory-evolved were established RNA, 2′-fluoroarabino nucleic acid (FANA), arabino (ANA), hexitol (HNA), threose...

10.1021/acssynbio.1c00048 article EN ACS Synthetic Biology 2021-05-24

Xeno-nucleic acid (XNA) aptamers based on evolvable non-natural genetic polymers hold enormous potential as future diagnostic and therapeutic agents. However, time-consuming costly procedures requiring the purification of individual XNA sequences produced by large-scale polymerase-mediated primer extension reactions pose a major bottleneck to discovery highly active motifs for biomedical applications. Here, we describe straightforward approach rapidly surveying binding properties identified...

10.1021/acssynbio.3c00189 article EN ACS Synthetic Biology 2023-07-06

10.1016/bs.mie.2023.04.014 article EN Methods in enzymology on CD-ROM/Methods in enzymology 2023-01-01

Abstract Synthetic genetics is an area of synthetic biology that aims to extend the properties heredity and evolution artificial genetic polymers, commonly known as xeno‐nucleic acids or XNAs. In addition establishing polymerases are able convert information back forth between DNA XNA, efforts underway construct XNAs with expanded chemical functionality. α‐L‐Threose nucleic acid (TNA), a type XNA recalcitrant nuclease digestion amenable Darwinian evolution, provides model system for...

10.1002/bip.23388 article EN Biopolymers 2020-07-02

Renewable and biodegradable glucans are in demand for use a variety of industries. Adenosine Diphosphate Glucose Pyrophosphorylase (ADPG PPase), an allosterically regulated enzyme, serves as the rate limiting step glucan biosynthesis is attractive target protein engineering to increase yield. The enzyme from Thermodesulfovibrio yellowstonii (Td.y) has been successfully expressed E. coli purification scheme that includes hydroxyapatite anion exchange chromatography optimized. inclusion 250 mM...

10.1096/fasebj.28.1_supplement.769.14 article EN The FASEB Journal 2014-04-01

ADPGlucose Pyrophosphorylase (ADPG PPase) catalyzes the rate‐limiting step of glucan biosynthesis in plants and bacteria. The successful engineering ADPG PPase will allow for production more renewable biodegradable carbon. Thermodesulfovibrio yellowstonii (Td.y) shows only ~30% identity to other bacterial forms enzyme; at positions E15, F18, F23, S25, S28 Td.y enzyme differs from consensus glycine rich (positions 9‐17) KRAKPAV regions 23‐29), areas known play roles activity allosteric...

10.1096/fasebj.28.1_supplement.769.9 article EN The FASEB Journal 2014-04-01

ADP-Glucose Pyrophosphorylase (ADPG PPase) catalyzes the rate limiting step of starch and glycogen biosynthesis in plants bacteria, respectively. Understanding structure-function relationships ADPG PPase can facilitate rational engineering this enzyme to increase glucan production. The from Thermodesulfovibrio yellowstonii (Td.y.) represents a diverse form with some novel properties that could be incorporated into highly active stable enzyme. Further, sequence alignment data indicate Td.y...

10.1096/fasebj.29.1_supplement.881.13 article EN The FASEB Journal 2015-04-01

Glucans serve as critical energy storage compounds in nearly all living organisms. Such renewable and biodegradable carbon sources are demand now from industry an eco‐friendly substitute for petroleum based products. ADP‐Glucose Pyrophosphorylase (ADPG PPase) is the enzyme that catalyzes rate limiting step of glucan biosynthesis plants bacteria, respectively. The novel Thermodesulfovibrio yellowstonii ( Td.y ) ADPG PPase, a thermophilic, sulfate‐reducing bacterium, has potential properties...

10.1096/fasebj.30.1_supplement.835.4 article EN publisher-specific-oa The FASEB Journal 2016-04-01

ADPGlucose pyrophosphorylase (ADPG PPase, glgC gene product) catalyzes the rate‐limiting step of glucan biosynthesis in plants and bacteria. Engineering this enzyme family will allow for increased production renewable carbon. The Thermodesulfovibrio yellostonii ( Td.y ) has been successfully cloned recombinant purified. This displays only ~30% identity to other characterized ADPG PPases harbors unusual sequences regions involved regulation. Molecular modeling studies revealed that was most...

10.1096/fasebj.27.1_supplement.1004.6 article EN The FASEB Journal 2013-04-01

Glucans such as starch serve energy storage compounds and renewable biodegradable carbon sources for use in industry. ADP‐Glucose Pyrophosphorylase (ADPG PPase) catalyzes the rate limiting step of glucan biosynthesis plants bacteria, respectively. The novel Thermodesulfovibrio yellowstonii ( Td.y ) ADPG PPase, from a thermophilic, sulfate‐reducing has potential properties that could lead to engineering very stable highly active form increase biomass yield. Sequence alignment data indicate...

10.1096/fasebj.31.1_supplement.765.19 article EN The FASEB Journal 2017-04-01
Coming Soon ...