ArticleBioMed research international2013
Interaction of human Dopa decarboxylase with L-Dopa: spectroscopic and kinetic studies as a function of pH.
Article in BioMed research international, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- α-Hydrazino Acids Inhibit Pyridoxal Phosphate-Dependent Decarboxylases via "Catalytically Correct" Ketoenamine Tautomers: A Special Motif for Chemical Biology and Drug Discovery?ACS catalysis · 2025Article
- The Role of Dopamine in Gastric Cancer-A Systematic Review of the Pathogenesis Phenomena Developments.Biomedicines · 2024Review
- Glial cells improve Parkinson's disease by modulating neuronal function and regulating neuronal ferroptosis.Frontiers in cell and developmental biology · 2024Review
- L-serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase.Protein science : a publication of the Protein Society · 2023Article
- Role of Protein Damage Inflicted by Dopamine Metabolites in Parkinson's Disease: Evidence, Tools, and Outlook.Chemical research in toxicology · 2022Review
- The novel P330L pathogenic variant of aromatic amino acid decarboxylase maps on the catalytic flexible loop underlying its crucial role.Cellular and molecular life sciences : CMLS · 2022Article
- Aromatic Amino Acid Decarboxylase Deficiency: The Added Value of Biochemistry.International journal of molecular sciences · 2021Review
- What We Know and What We Need to Know about Aromatic and Cationic Biogenic Amines in the Gastrointestinal Tract.Foods (Basel, Switzerland) · 2018Review
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5 authors.
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Abstract
Human Dopa decarboxylase (hDDC), a pyridoxal 5'-phosphate (PLP) enzyme, displays maxima at 420 and 335 nm and emits fluorescence at 384 and 504 nm upon excitation at 335 nm and at 504 nm when excited at 420 nm. Absorbance and fluorescence titrations of hDDC-bound coenzyme identify a single pK(spec) of ~7.2. This pK(spec) could not represent the ionization of a functional group on the Schiff base but that of an enzymic residue governing the equilibrium between the low- and the high-pH forms of the internal aldimine. During the reaction of hDDC with L-Dopa, monitored by stopped-flow spectrophotometry, a 420 nm band attributed to the 4'-N-protonated external aldimine first appears, and its decrease parallels the emergence of a 390 nm peak, assigned to the 4'-N-unprotonated external aldimine. The pH profile of the spectral change at 390 nm displays a pK of 6.4, a value similar to that (~6.3) observed in both k(cat) and k(cat)/K(m) profiles. This suggests that this pK represents the ESH(+) → ES catalytic step. The assignment of the pKs of 7.9 and 8.3 observed on the basic side of k(cat) and the PLP binding affinity profiles, respectively, is also analyzed and discussed.
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