1.5.5.2: proline dehydrogenase
This is an abbreviated version!
For detailed information about proline dehydrogenase, go to the full flat file.
Word Map on EC 1.5.5.2
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1.5.5.2
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putas
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schizophrenia
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pyrroline-5-carboxylate
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delta1-pyrroline-5-carboxylate
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flavoenzyme
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psycho
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hyperprolinemia
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microdeletion
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schizoaffective
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2-acetyl-1-pyrroline
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rgs4
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velocardiofacial
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proline-dependent
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digeorge
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dysbindin
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fragrant
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prolidase
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synthesis
- 1.5.5.2
-
putas
-
schizophrenia
- pyrroline-5-carboxylate
- delta1-pyrroline-5-carboxylate
-
flavoenzyme
-
psycho
-
hyperprolinemia
-
microdeletion
-
schizoaffective
-
2-acetyl-1-pyrroline
- rgs4
-
velocardiofacial
-
proline-dependent
-
digeorge
-
dysbindin
-
fragrant
- prolidase
- synthesis
Reaction
Synonyms
bifunctional dye-linked L-proline/NADH dehydrogenase complex, dye-linked L-proline dehydrogenase, EC 1.5.99.8, FAD-dependent L-proline oxidoreductase, JcProDH, L-proline dehydrogenase, L-proline:FAD oxidoreductase, PdhB, PDHbeta, PF1246, PF1798, PH1364, PH1751, PRODH, proDH-B1, proDH-B2, PRODH/POX, ProDH1, proline dehydrogenase, proline dehydrogenase 1, proline dehydrogenase/oxidase, proline oxidase, proline/P5C dehydrogenase, prub, PutA, PutA flavoprotein, PutA proline dehydrogenase, Tc00.1047053506411.30, TcPRODH, TK0117, TK0122, TPpdhbeta, TtProDH
ECTree
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Localization
Localization on EC 1.5.5.2 - proline dehydrogenase
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transcriptional induction of the enzyme causes changes in expression levels of other mitochondrial enzymes. Activity of glutamate dehydrogenase is substantially increased, and activity of D-lactate dehydrogenase is increased
co-localization with the electron transport chain on the inner membrane of the mitochondria
co-localization with the electron transport chain on the inner membrane of the mitochondria
TcPRODH is associated with the mitochondrial inner membrane, identification of a predicted N-terminal mitochondrial targeting signal, followed by a putative transmembrane alpha helix spanning domain
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TcPRODH is associated with the mitochondrial inner membrane, identification of a predicted N-terminal mitochondrial targeting signal, followed by a putative transmembrane alpha helix spanning domain
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isozyme ProDH1 forms part of a low-molecular-mass (70-140 kDa) complex in the mitochondrial membrane, proteomic analysis