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Literature summary extracted from

  • Nakanishi, N.; Hasegawa, H.; Yamada, S.; Akino, M.
    Purification and physicochemical properties of NADPH-specific dihydropteridine reductase from bovine and human livers (1986), J. Biochem., 99, 635-644.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.34 35000
-
 2 * 35000, NADPH-specific liver enzyme, SDS-PAGE Homo sapiens
1.5.1.34 35000
-
 2 * 35000, NADPH-specific liver enzyme, SDS-PAGE Bos taurus
1.5.1.34 65000
-
 equilibrium centrifugation, NADPH-specific liver enzyme Bos taurus
1.5.1.34 68000
-
 NADPH-specific enzyme, gel filtration Bos taurus
1.5.1.34 69000
-
 NADPH-specific liver enzyme, gel filtration Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.34 Bos taurus
-
-
-
1.5.1.34 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.34
-
 Homo sapiens
1.5.1.34
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.34 liver
-
 Homo sapiens
-
1.5.1.34 liver
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.34 0.706
-
 NADPH-specific liver enzyme Homo sapiens
1.5.1.34 0.972
-
 NADPH-specific liver enzyme Bos taurus

Subunits

EC Number Subunits Comment Organism
1.5.1.34 dimer 2 * 35000, NADPH-specific liver enzyme, SDS-PAGE Homo sapiens
1.5.1.34 dimer 2 * 35000, NADPH-specific liver enzyme, SDS-PAGE Bos taurus

Synonyms

EC Number Synonyms Comment Organism
1.5.1.34 More enzyme is not identical with dihydrofolate reductase Homo sapiens
1.5.1.34 More enzyme is not identical with dihydrofolate reductase Bos taurus
1.5.1.34 More NADPH-specific dihydropteridine reductase and NADH-dihydropteridine reductase have no common antigenic determinants, and show different physicochemical properties Homo sapiens
1.5.1.34 More NADPH-specific dihydropteridine reductase and NADH-dihydropteridine reductase have no common antigenic determinants, and show different physicochemical properties Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.34 NADH
-
 Homo sapiens
1.5.1.34 NADH liver: 2 distinct dihydropteridine reductases which catalyze the conversion of the quinonoid dihydropteridine to tetrahydropterin: NADH-dihydropteridine reductase, DPR, utilizes NADH as a better substrate than NADPH, NADPH-specific dihydropteridine reductase, TPR, shows strict specificity for NADPH Bos taurus
1.5.1.34 NADPH
-
 Homo sapiens
1.5.1.34 NADPH liver: 2 distinct dihydropteridine reductases which catalyze the conversion of the quinonoid dihydropteridine to tetrahydropterin: NADH-dihydropteridine reductase, DPR, utilizes NADH as a better substrate than NADPH, NADPH-specific dihydropteridine reductase, TPR, shows strict specificity for NADPH Bos taurus