A Nucleophilic Activity‐Based Probe Enables Profiling of PLP‐Dependent Enzymes
Sign Up to like & getrecommendations! Published in 2023 at "ChemBioChem"
DOI: 10.1002/cbic.202200669
Abstract: PLP‐dependent enzymes represent an important class of highly “druggable” enzymes that perform a wide array of critical reactions to support all organisms. Inhibition of individual members of this family of enzymes has been validated as… read more here.
Keywords: dependent enzymes; plp dependent; nucleophilic activity; activity based ... See more keywords
A single amino acid substitution converts a histidine decarboxylase to an imidazole acetaldehyde synthase.
Sign Up to like & getrecommendations! Published in 2020 at "Archives of biochemistry and biophysics"
DOI: 10.1016/j.abb.2020.108551
Abstract: Histidine decarboxylase (HDC; EC 4.1.1.22), an enzyme that catalyzes histamine synthesis with high substrate specificity, is a member of the group II pyridoxal 5'-phosphate (PLP) -dependent decarboxylase family. Tyrosine is a conserved residue among group… read more here.
Keywords: histidine decarboxylase; decarboxylase; amino acid; acetaldehyde synthase ... See more keywords
A Fold Type II PLP-Dependent Enzyme from Fusobacterium nucleatum Functions as a Serine Synthase and Cysteine Synthase.
Sign Up to like & getrecommendations! Published in 2021 at "Biochemistry"
DOI: 10.1021/acs.biochem.0c00902
Abstract: Serine synthase (SS) from Fusobacterium nucleatum is a fold type II pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the β-replacement of l-cysteine with water to form l-serine and H2S. Herein, we show that SS can also… read more here.
Keywords: synthase; cysteine; fold type; serine synthase ... See more keywords
Pyridoxal 5'-Phosphate (PLP)-Dependent β- and γ-Substitution Reactions Forming Nonproteinogenic Amino Acids in Natural Product Biosynthesis.
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DOI: 10.1021/acs.jnatprod.4c01226
Abstract: Living organisms synthesize various nonproteinogenic amino acids (NPAAs) as the building blocks of natural products. These NPAAs are often biosynthesized by pyridoxal 5'-phosphate (PLP)-dependent enzymes, which catalyze β- or γ- substitutions. These enzymes contribute to… read more here.
Keywords: plp; nonproteinogenic amino; amino acids; pyridoxal phosphate ... See more keywords
Catalytic Roles of Coenzyme Pyridoxal-5'-phosphate (PLP) in PLP-dependent Enzymes: Reaction Pathway for Methionine-γ-lyase-catalyzed L-methionine Depletion.
Sign Up to like & getrecommendations! Published in 2020 at "ACS catalysis"
DOI: 10.1021/acscatal.9b03907
Abstract: Pyridoxal-5'-phosphate (PLP), the active form of vitamin B6, is an important and versatile coenzyme involved in a variety of enzymatic reactions, accounting for about 4% of all classified activities. However, the detailed catalytic reaction pathways… read more here.
Keywords: plp; phosphate plp; pyridoxal phosphate; dependent enzymes ... See more keywords
Snapshots of the Catalytic Cycle of an O2, Pyridoxal Phosphate-Dependent Hydroxylase.
Sign Up to like & getrecommendations! Published in 2018 at "ACS chemical biology"
DOI: 10.1021/acschembio.8b00039
Abstract: Enzymes that catalyze hydroxylation of unactivated carbons normally contain heme and nonheme iron cofactors. By contrast, how a pyridoxal phosphate (PLP)-dependent enzyme could catalyze such a hydroxylation was unknown. Here, we investigate RohP, a PLP-dependent… read more here.
Keywords: snapshots catalytic; plp dependent; pyridoxal phosphate; catalytic cycle ... See more keywords
Discovery and Characterization of Pyridoxal 5'-Phosphate-Dependent Cycloleucine Synthases.
Sign Up to like & getrecommendations! Published in 2024 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.4c02142
Abstract: Pyridoxal 5'-phosphate (PLP)-dependent enzymes are the most versatile biocatalysts for synthesizing nonproteinogenic amino acids. α,α-Disubstituted quaternary amino acids, such as 1-aminocyclopentane-1-carboxylic acid (cycloleucine), are useful building blocks for pharmaceuticals. In this study, starting with the… read more here.
Keywords: pyridoxal phosphate; cycloleucine synthases; plp dependent; cycloleucine ... See more keywords
Structural Insights into the Mechanism of a Polyketide Synthase Thiocysteine Lyase Domain.
Sign Up to like & getrecommendations! Published in 2024 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.4c11656
Abstract: Polyketide synthases (PKSs) are renowned for the structural diversity of the polyketide natural products they produce, but sulfur-containing functionalities are rarely installed by PKSs. We previously characterized thiocysteine lyase (SH) domains involved in the biosynthesis… read more here.
Keywords: natural products; thiocysteine lyase; insights mechanism; structural insights ... See more keywords
Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase from Desulfomonile tiedjei
Sign Up to like & getrecommendations! Published in 2025 at "International Journal of Molecular Sciences"
DOI: 10.3390/ijms26178536
Abstract: Understanding the structure–function relationships of pyridoxal-5′-phosphate (PLP)-dependent transaminases is key to advancing pyridoxal-phosphate-dependent catalysis and engineering transaminases for industrial applications. Despite our extensive knowledge of PLP-dependent enzymatic reactions, engineering transaminase activity and stability remains challenging.… read more here.
Keywords: transaminase; plp; transaminase desulfomonile; plp dependent ... See more keywords