Retinal dehydrogenase 1; Can convert/oxidize retinaldehyde to retinoic acid. Binds free retinal and cellular retinol-binding protein-bound retinal (By similarity). May have a broader specificity and oxidize other aldehydes in vivo.

Retinal dehydrogenase 2; Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. Displays complete lack of activity with citral (By similarity). Belongs to the aldehyde dehydrogenase family.

Retinal dehydrogenase 1; Can convert/oxidize retinaldehyde to retinoic acid. Binds free retinal and cellular retinol-binding protein-bound retinal (By similarity). May have a broader specificity and oxidize other aldehydes in vivo.

Aldehyde dehydrogenase family 1 member A3; NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid. Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde. Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region (By similarity).

Retinal dehydrogenase 2; Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. Displays complete lack of activity with citral (By similarity). Belongs to the aldehyde dehydrogenase family.

Retinal dehydrogenase 1; Can convert/oxidize retinaldehyde to retinoic acid. Binds free retinal and cellular retinol-binding protein-bound retinal (By similarity). May have a broader specificity and oxidize other aldehydes in vivo.

Retinal dehydrogenase 2; Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. Displays complete lack of activity with citral (By similarity). Belongs to the aldehyde dehydrogenase family.

Aldehyde dehydrogenase family 1 member A3; NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid. Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde. Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region (By similarity).

Aldehyde dehydrogenase family 1 member A3; NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid. Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde. Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region (By similarity).

Retinal dehydrogenase 1; Can convert/oxidize retinaldehyde to retinoic acid. Binds free retinal and cellular retinol-binding protein-bound retinal (By similarity). May have a broader specificity and oxidize other aldehydes in vivo.

Aldehyde dehydrogenase family 1 member A3; NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid. Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde. Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region (By similarity).

Retinal dehydrogenase 2; Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. Displays complete lack of activity with citral (By similarity). Belongs to the aldehyde dehydrogenase family.

Bifunctional purine biosynthesis protein PURH, N-terminally processed; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family.

Dihydrofolate reductase; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.

Bifunctional purine biosynthesis protein PURH, N-terminally processed; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family.

Dihydrofolate reductase 2, mitochondrial; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Binds its own mRNA and that of DHFR.

Bifunctional purine biosynthesis protein PURH, N-terminally processed; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family.

Thymidylate kinase; Catalyzes the conversion of dTMP to dTDP; Belongs to the thymidylate kinase family.

Bifunctional purine biosynthesis protein PURH, N-terminally processed; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family.

Trifunctional purine biosynthetic protein adenosine-3; Phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase; In the central section; belongs to the AIR synthase family.

Bifunctional purine biosynthesis protein PURH, N-terminally processed; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family.

Methylenetetrahydrofolate reductase; Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co-substrate for homocysteine remethylation to methionine.

Bifunctional purine biosynthesis protein PURH, N-terminally processed; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family.

Thymidylate synthase; Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.

Dihydrofolate reductase; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.

Bifunctional purine biosynthesis protein PURH, N-terminally processed; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family.

Dihydrofolate reductase; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.

Dihydrofolate reductase 2, mitochondrial; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Binds its own mRNA and that of DHFR.

Dihydrofolate reductase; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.

Thymidylate kinase; Catalyzes the conversion of dTMP to dTDP; Belongs to the thymidylate kinase family.

Dihydrofolate reductase; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.

Trifunctional purine biosynthetic protein adenosine-3; Phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase; In the central section; belongs to the AIR synthase family.

Dihydrofolate reductase; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.

Methylenetetrahydrofolate reductase; Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co-substrate for homocysteine remethylation to methionine.

Dihydrofolate reductase; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.

Thymidine kinase 2, mitochondrial; Phosphorylates thymidine, deoxycytidine, and deoxyuridine in the mitochondrial matrix. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on TK2 and DGUOK. Widely used as target of antiviral and chemotherapeutic agents; Belongs to the DCK/DGK family.

Dihydrofolate reductase; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.

Thymidylate synthase; Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.

Dihydrofolate reductase 2, mitochondrial; Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Binds its own mRNA and that of DHFR.

Bifunctional purine biosynthesis protein PURH, N-terminally processed; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family.