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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Crystallization
Crystallization on EC 1.5.5.2 - proline dehydrogenase
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2.15 A resolution structure of the PRODH inactivated by N-propargylglycine. The initial events involved in broadcasting the reduced flavin state to the distal membrane-binding domain include major reorganization of the flavin ribityl chain, severe butterfly bending of the isoalloxazine ring, and disruption of an electrostatic network involving the flavin N(5) atom, Arg431, and Asp370. The active site is incompletely assembled in the absence of the substrate, and the binding of proline draws together conserved residues in helix 8 and the beta1-alphal loop to complete the active site
sitting-drop vaor diffusion method, structures of the PutA PRODH domain complexed with competitive inhibitors, acetate, L-lactate and L-tetrahydro-2-furoic acid
inhibitor thiazolidine-2-carboxylate covalently binds to the N5 of the FAD in the PRODH domain. The modified FAD exhibits a large butterfly bend angle
purified TtProDH mutant variant DELTAABC lacking helices alphaA, alphaB and alphaC, X-ray diffraction structure determination and analysis at 2.2 A resolution