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
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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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Cofactor
Cofactor on EC 1.5.5.2 - proline dehydrogenase
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coenzyme Q1 is electron acceptor for PRODH/POX, which passes electrons directly to coenzyme Q1 (CoQ1) RODH/POX binds directly to CoQ1 without the formation of a tertiary complex. The transfer of electrons from proline to CoQ1 by PRODH/POX is dependent on downstream electron transfer from CoQ1 to Complexes III and IV
coenzyme Q1
coenzyme Q1 is electron acceptor for PRODH/POX, which passes electrons directly to coenzyme Q1 (CoQ1) RODH/POX binds directly to CoQ1 without the formation of a tertiary complex. The transfer of electrons from proline to CoQ1 by PRODH/POX is dependent on downstream electron transfer from CoQ1 to Complexes III and IV
FAD
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FAD may be released by 1 M KBr, apoprotein has no proline dehydrogenase activity but may be restored by external addition of FAD
FAD
determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252
FAD
enzyme-bound, dependent on. Addition of excess FAD hardly improves the enzyme activity, confirming that the enzyme is fully saturated with FAD
FAD
proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group
FAD
TcPRODH is a FAD-dependent protein, key residues involved in cofactor (FAD) binding are Arg431 and Glu559
FMN
proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group
the recombinant holo form of MBP-tagged TtProDH, as produced in Escherichia coli TOP10 cells, contains about three times more FMN than FAD. The crystal structure of TtProDH variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, shows no electron density for an AMP moiety of the cofactor. ProDH adopts a distorted (betalpha)8 TIM-barrel fold and is the only known TIM-barrel enzyme that contains an FAD cofactor. One cofactor molecule per enzyme subunit
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additional information
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the recombinant holo form of MBP-tagged TtProDH, as produced in Escherichia coli TOP10 cells, contains about three times more FMN than FAD. The crystal structure of TtProDH variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, shows no electron density for an AMP moiety of the cofactor. ProDH adopts a distorted (betalpha)8 TIM-barrel fold and is the only known TIM-barrel enzyme that contains an FAD cofactor. One cofactor molecule per enzyme subunit
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