EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.1.34 | gene Dhpr, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Bombyx mori |
4.2.1.96 | PCD sequence comparisons and phylogenetic tree, enzyme expression analysis | Bombyx mori |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.5.1.34 | additional information | generation of lethal mutants of a65 and a60 strains. For a65 (leml/leml) and a60 (al/al), the reaction rate of total proteins is 0.373 and 3.352 microM/min/mg protein, respectively. The expression of BmDhpr is especially activated in the brain and sexual glands of lem mutant and the homozygous lethal mutant of al mutant | Bombyx mori |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.1.34 | 0.0314 | - |
NADH | pH 7.4, 22°C, recombinant enzyme | Bombyx mori | |
1.5.1.34 | 0.0729 | - |
NADPH | pH 7.4, 22°C, recombinant enzyme | Bombyx mori | |
1.5.1.34 | 0.821 | - |
6,7-dimethyl-7,8-dihydropteridine | pH 7.4, 22°C, recombinant enzyme | Bombyx mori |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.34 | a 6,7-dihydropteridine + NAD(P)H + H+ | Bombyx mori | - |
a 5,6,7,8-tetrahydropteridine + NAD(P)+ | - |
? | |
4.2.1.96 | (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin | Bombyx mori | - |
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.34 | Bombyx mori | - |
several strains | - |
4.2.1.96 | Bombyx mori | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.5.1.34 | native enzyme from fifth larval instar of p50 and ah09 strains, recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration | Bombyx mori |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.5.1.34 | brain | - |
Bombyx mori | - |
1.5.1.34 | fat body | larvaeal | Bombyx mori | - |
1.5.1.34 | larva | - |
Bombyx mori | - |
1.5.1.34 | additional information | the expression of BmDhpr is especially activated in the brain and sexual glands of lem mutant and the homozygous lethal mutant of al mutant | Bombyx mori | - |
1.5.1.34 | sexual gland | - |
Bombyx mori | - |
4.2.1.96 | brain | - |
Bombyx mori | - |
4.2.1.96 | imago | - |
Bombyx mori | - |
4.2.1.96 | larva | third, forth, and fifth instar | Bombyx mori | - |
4.2.1.96 | additional information | PCD enzyme transcription profiles in different strains, expression analysis, overview. BmPcd is expressed almost throughout the whole life cycle | Bombyx mori | - |
4.2.1.96 | ovariotestis | - |
Bombyx mori | - |
4.2.1.96 | pupa | high expression level | Bombyx mori | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.34 | 6,7-dimethyl-7,8-dihydropteridine + NADH + H+ | NADH is preferred in vitro compared to NADPH | Bombyx mori | 6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD+ | - |
? | |
1.5.1.34 | a 6,7-dihydropteridine + NAD(P)H + H+ | - |
Bombyx mori | a 5,6,7,8-tetrahydropteridine + NAD(P)+ | - |
? | |
1.5.1.34 | a 6,7-dihydropteridine + NADPH + H+ | - |
Bombyx mori | a 5,6,7,8-tetrahydropteridine + NADP+ | - |
? | |
4.2.1.96 | (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin | - |
Bombyx mori | (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.5.1.34 | ? | x * 17900, about, sequence calculation | Bombyx mori |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.1.34 | BmDhpr | - |
Bombyx mori |
1.5.1.34 | DHPR | - |
Bombyx mori |
1.5.1.34 | dihydropteridine reductase | - |
Bombyx mori |
4.2.1.96 | PCD | - |
Bombyx mori |
4.2.1.96 | Pterin-4a-carbinolamine dehydratase | - |
Bombyx mori |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.1.34 | 22 | - |
assay at room temperature | Bombyx mori |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.5.1.34 | 7.4 | - |
assay at | Bombyx mori |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.34 | additional information | the recombinant BmDHPR exhibits high enzymatic activity and more suitable parameters to the coenzyme of NADH in vitro | Bombyx mori | |
1.5.1.34 | NAD(P)H | - |
Bombyx mori |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
1.5.1.34 | Bombyx mori | sequence calculation | - |
9.9 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.1.34 | malfunction | tetrahydrobiopterin deficiency is associated with numerous metabolic syndromes and neuropsychological disorders | Bombyx mori |
1.5.1.34 | metabolism | the enzyme is involved in the De novo pathway and regeneration pathway of tetrahydrobiopterin biosynthesis | Bombyx mori |
1.5.1.34 | physiological function | the enzyme is important in the regeneration pathway of tetrahydrobiopterin, BH4. Tetrahydrobiopterin (BH4) is an essential cofactor of aromatic amino acid hydroxylases and nitric oxide synthase so that BH4 plays a key role in many biological processes | Bombyx mori |
4.2.1.96 | malfunction | in mutant phenotype lemon, the expression of BmDhpr is activated in the brain and sexual glands while BmPcd is expressed in a wider special pattern when the de novo pathway of BH4 is missing | Bombyx mori |
4.2.1.96 | metabolism | pterin-4a-carbinolamine dehydratase (PCD, BmPcd) and dihydropteridine reductase (DHPR, BmDhpr) might normally act in the regeneration pathway of Bombyx mori | Bombyx mori |
4.2.1.96 | physiological function | the regeneration pathway (RPB) of tetrahydrobiopterin (BH4), an essential cofactor of aromatic amino acid hydroxylases and nitric oxide synthase playing a key role in many biological processes, in Bombyx mori. The enzyme is involved in the insect BH4 biosynthetic networks, overview | Bombyx mori |