Page last updated: 2024-08-17

hydroxyproline and flavin-adenine dinucleotide

hydroxyproline has been researched along with flavin-adenine dinucleotide in 3 studies

Research

Studies (3)

Timeframe	Studies, this research(%)	All Research%
pre-1990	2 (66.67)	18.7374
1990's	0 (0.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	1 (33.33)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Hayaishi, O; Nozaki, M	1
Soda, K	1
Holmes, RP; Johnson, LC; Jönsson, TJ; Lowther, WT; Parsonage, D; Summitt, CB	1

Reviews

1 review(s) available for hydroxyproline and flavin-adenine dinucleotide

Article	Year
[Amino acid racemases (author's transl)]. Seikagaku. The Journal of Japanese Biochemical Society, 1974, Volume: 46, Issue:5 Topics: Adenosine Triphosphate; Alanine; Amino Acid Isomerases; Arginine; Chemical Phenomena; Chemistry; Coenzymes; Flavin-Adenine Dinucleotide; Glutamine; Hydrogen-Ion Concentration; Hydroxyproline; Magnetic Resonance Spectroscopy; Molecular Weight; Phenylalanine; Pyridoxal Phosphate; Spectrophotometry	1974

Article

Year

[Amino acid racemases (author's transl)].

Seikagaku. The Journal of Japanese Biochemical Society, 1974, Volume: 46, Issue:5

Topics: Adenosine Triphosphate; Alanine; Amino Acid Isomerases; Arginine; Chemical Phenomena; Chemistry; Coenzymes; Flavin-Adenine Dinucleotide; Glutamine; Hydrogen-Ion Concentration; Hydroxyproline; Magnetic Resonance Spectroscopy; Molecular Weight; Phenylalanine; Pyridoxal Phosphate; Spectrophotometry

1974

Other Studies

2 other study(ies) available for hydroxyproline and flavin-adenine dinucleotide

Article	Year
Nature and mechanisms of oxygenases. Science (New York, N.Y.), 1969, Apr-25, Volume: 164, Issue:3878 Topics: Amino Acids; Bacteria; Biotransformation; Catalysis; Catechol Oxidase; Chemical Phenomena; Chemistry; Cholesterol; Collagen; Dihydroxyphenylalanine; Flavin-Adenine Dinucleotide; Hydroxyproline; Lysine; NAD; Oxygen; Oxygenases; Phenylalanine; Plants; Prostaglandins; Squalene; Tryptophan Oxygenase; Tyrosine	1969
Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria. The Biochemical journal, 2015, Mar-01, Volume: 466, Issue:2 Topics: Biocatalysis; Catalytic Domain; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Flavoproteins; Furans; Humans; Hydroxyproline; Hyperoxaluria, Primary; Ligands; Models, Molecular; Mutant Proteins; Peptide Fragments; Proline; Proline Oxidase; Protein Conformation; Recombinant Proteins; Substrate Specificity; Terminology as Topic; Ubiquinone	2015

Article

Year

Nature and mechanisms of oxygenases.

Science (New York, N.Y.), 1969, Apr-25, Volume: 164, Issue:3878

Topics: Amino Acids; Bacteria; Biotransformation; Catalysis; Catechol Oxidase; Chemical Phenomena; Chemistry; Cholesterol; Collagen; Dihydroxyphenylalanine; Flavin-Adenine Dinucleotide; Hydroxyproline; Lysine; NAD; Oxygen; Oxygenases; Phenylalanine; Plants; Prostaglandins; Squalene; Tryptophan Oxygenase; Tyrosine

1969

Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria.

The Biochemical journal, 2015, Mar-01, Volume: 466, Issue:2

Topics: Biocatalysis; Catalytic Domain; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Flavoproteins; Furans; Humans; Hydroxyproline; Hyperoxaluria, Primary; Ligands; Models, Molecular; Mutant Proteins; Peptide Fragments; Proline; Proline Oxidase; Protein Conformation; Recombinant Proteins; Substrate Specificity; Terminology as Topic; Ubiquinone

2015