A5014663468- Porphyrin Metabolism and Disorders
- Biochemical and Molecular Research
- RNA modifications and cancer
- Folate and B Vitamins Research
- RNA and protein synthesis mechanisms
- RNA Research and Splicing
- Ion channel regulation and function
- Heme Oxygenase-1 and Carbon Monoxide
- Enzyme function and inhibition
- Metal complexes synthesis and properties
- Enzyme Production and Characterization
University of Michigan
2019-2023
New England Biolabs (China)
2023
The University of Texas at Austin
2018
Itaconate brings metalloenzyme to a halt Controlled radicals enable unusual enzymatic transformations, but radical generation and management require dedicated systems. Ruetz et al. investigated how the immunometabolite itaconate might undermine these intricate systems inhibit propionate metabolism, crucial metabolic pathway in pathogenic Mycobacterium tuberculosis (Mtb) (see Perspective by Boal). They found that coenzyme A (CoA) derivative of can irreversibly enzyme methylmalonyl-CoA mutase...
Significance Pseudouridine is among the most-abundant RNA modifications. We present a framework for conceptualizing how eukaryotic pseudouridine synthases select their substrates. This work reveals structure of yeast synthase 7 (Pus7) and presents cell-based biochemical investigations enzyme binding activity. demonstrate that Pus7 interacts promiscuously with RNAs containing UG U AR sequences. Our observations raise question why these enzymes only modify <5% sequences in transcriptome,...
Cobalamin-dependent methionine synthase (MS) is a key enzyme in and folate one-carbon metabolism. MS large multi-domain protein capable of binding activating three substrates: homocysteine, folate, S-adenosylmethionine for methylation. Achieving chemically distinct methylations necessitates significant domain rearrangements to facilitate substrate access the cobalamin cofactor at right time. The conformations required each reaction have eluded structural characterization as its inherently...
We report the synthesis and application of a small molecule probe for carbonic anhydrase (CA) to track holo-CA in cell lysates live-cell models zinc dyshomeostasis. The displays 12-fold increase fluorescence upon binding bovine CA also responds human isoforms.
Abstract Cobalamin-dependent methionine synthase (MS) is a key enzyme in and folate one-carbon metabolism. MS large multi-domain protein capable of binding activating three substrates: homocysteine, folate, S -adenosylmethionine for methylation. Achieving chemically distinct methylations necessitates significant domain rearrangements to facilitate substrate access the cobalamin cofactor at right time. The conformations required each reaction have eluded structural characterization as its...
Abstract Cobalamin-dependent methionine synthase (MS) is a key enzyme in and folate one-carbon metabolism. MS large multi-domain protein capable of binding activating three substrates: homocysteine, folate, S -adenosylmethionine for methylation. Achieving chemically distinct methylations necessitates significant domain rearrangements to facilitate substrate access the cobalamin cofactor at right time. The conformations required each reaction have eluded structural characterization as its...