Publications by authors named "Hyeonjeong Yu"
Crystal structures of cystathionine β-lyase and cystathionine β-lyase like protein from Bacillus cereus ATCC 14579.
Biochem Biophys Res Commun
January 2025
Article Synopsis
- Cystathionine β-lyase (CBL) and cystathionine β-lyase-like protein (CBLP) are important enzymes in methionine biosynthesis in Bacillus cereus, converting cystathionine into homocysteine and pyruvate.* -
- The study revealed that BcCBLP has a higher catalytic efficiency than BcCBL, and their crystal structures showed BcCBL forms a tetramer while BcCBLP forms a dimer, suggesting different functional roles.* -
- These findings enhance our understanding of the structural diversity and regulatory functions of these enzymes, contributing valuable knowledge to PLP-dependent enzymatic processes.*
Since the discovery of l-glutamate-producing , it has evolved to be an industrial workhorse. For biobased chemical production, suppling sufficient amounts of the NADPH cofactor is crucial. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme that converts glyceraldehyde-3-phosphate (G3P) to 1,3-bisphosphoglycerate and produces NADH, is a major prospective solution for the cofactor imbalance issue.
View Article and Find Full Text PDF() has been considered a very important and meaningful industrial microorganism for the production of amino acids worldwide. To produce amino acids, cells require nicotinamide adenine dinucleotide phosphate (NADPH), which is a biological reducing agent. The pentose phosphate pathway (PPP) can supply NADPH in cells via the 6-phosphogluconate dehydrogenase (6PGD) enzyme, which is an oxidoreductase that converts 6-phosphogluconate (6PG) to ribulose 5-phosphate (Ru5P), to produce NADPH.
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