A5073092786- Enzyme Catalysis and Immobilization
- Protein Structure and Dynamics
- Biochemical and Molecular Research
- Enzyme Production and Characterization
- Amino Acid Enzymes and Metabolism
- HIV/AIDS drug development and treatment
- Enzyme Structure and Function
- Mass Spectrometry Techniques and Applications
- Carbohydrate Chemistry and Synthesis
- Microbial Metabolic Engineering and Bioproduction
- Analytical Chemistry and Chromatography
- Receptor Mechanisms and Signaling
- Biopolymer Synthesis and Applications
- Catalytic C–H Functionalization Methods
- Hemoglobin structure and function
- Photoreceptor and optogenetics research
- Cassava research and cyanide
- Biochemical and Structural Characterization
- Oxidative Organic Chemistry Reactions
- Legume Nitrogen Fixing Symbiosis
- Innovative Microfluidic and Catalytic Techniques Innovation
- Photosynthetic Processes and Mechanisms
- Food Quality and Safety Studies
- Adenosine and Purinergic Signaling
- Tryptophan and brain disorders
QB3
2017-2024
University of California, Berkeley
2017-2024
Beijing University of Chemical Technology
2012-2020
Flavanone derivatives utilize the fundamental flavanone framework to enhance and target distinct bioactivities, rendering them valuable precursors in synthesis development of pharmaceuticals. Here we explore enzyme-catalyzed intramolecular C(sp3)-H...
A novel (+)-γ-lactamase used for the resolution of racemic γ-lactam from Bradyrhizobium japonicum USDA 6 was found as a result sequence-structure guided genome mining. It consists 409 amino acids, only 49% which are identical to acid sequences known Sulfolobus solfataricus. This is third gene be reported.
Human catechol
Proteins are intrinsically flexible macromolecules that undergo internal motions with time scales spanning femtoseconds to milliseconds. These fluctuations implicated in the optimization of reaction barriers for enzyme catalyzed reactions. Time, temperature, and mutation dependent hydrogen–deuterium exchange coupled mass spectrometry (HDX-MS) has been previously employed identify spatially resolved, catalysis-linked dynamical regions enzymes. We now extend this technique pursue correlation...
Abstract 4-Hydroxyphenylacetate 3-hydroxylase (EcHpaB) from Escherichia coli is capable of efficient ortho -hydroxylation a wide range phenolic compounds and demonstrates great potential for broad chemoenzymatic applications. To understand the structural mechanistic basis its catalytic versatility, we elucidated crystal structure EcHpaB by X-ray crystallography, which revealed unique loop covering active site. We further performed mutagenesis studies this to probe role in substrate...
To produce promising biocatalysts, natural enzymes often need to be engineered increase their catalytic performance. In this study, the enantioselectivity and thermostability of a (+)-γ-lactamase from Microbacterium hydrocarbonoxydans as catalyst in kinetic resolution Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) were improved. Enantiomerically pure (-)-Vince is key synthon synthesis antiviral drugs, such carbovir abacavir, which are used fight against HIV hepatitis B virus. The work was...
Abstract (+)-γ-lactamase catalyzes the specific hydrolysis of (+)-γ-lactam out racemic γ-lactam (2-Azabicyclo[2.2.1]hept-5-en-3-one) to leave optically pure (−)-γ-lactam, which is key building block antiviral drugs such as carbovir and abacavir. However, no structural data has been reported on how enzymes bind γ-lactams achieve their enantioselectivities. We previously identified an isochorismatase-like hydrolase (IHL, Mh33H4-5540) with activity, constitutes a novel family γ-lactamase. Here,...
Murine adenosine deaminase (mADA) is a prototypic system for studying the thermal activation of active site chemistry within TIM barrel family enzyme reactions. Previous temperature-dependent hydrogen–deuterium exchange studies under various conditions have identified interconnected networks heat transfer from opposing protein–solvent interfaces to residues in mADA. One these contains solvent-exposed helix–loop–helix moiety that presents hydrophobic face its long α-helix backside bound...
ADVERTISEMENT RETURN TO ISSUEPREVAddition/CorrectionNEXTORIGINAL ARTICLEThis notice is a correctionCorrection to "Hydrogen–Deuterium Exchange within Adenosine Deaminase, TIM Barrel Hydrolase, Identifies Networks for Thermal Activation of Catalysis"Shuaihua GaoShuaihua GaoMore by Shuaihua Gaohttp://orcid.org/0000-0003-3303-3856, Emily J. ThompsonEmily ThompsonMore Thompsonhttp://orcid.org/0000-0003-4624-7239, Samuel L. BarrowSamuel BarrowMore Barrow, Wenju ZhangWenju ZhangMore Zhang, Anthony...