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
-
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
- 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
Advanced search results
Engineering
Engineering on EC 1.5.5.2 - proline dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
D370A
-
mutant form of PutA86-601. The ratio of turnover-number to Km-value is 2.8fold lower than the ratio of the wild-type PutA86-601
D370A/Y540F
-
mutant form of PutA86-601. The ratio of turnover-number to Km-value is 15fold lower than the ratio of the wild-type PutA86-601
L432P
mutant form of PutA86-669, 5fold decrease in turnover-number and a severe loss in thermostability
W194F
-
mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 50%
W194F/W211F
-
mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 95%
W211F
-
mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 80%
Y540F
-
mutant form of PutA86-601. The ratio of turnover-number to Km-value is 5.8fold lower than the ratio of the wild-type PutA86-601
Y203F
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
F10E/L12E
additional information
construction of a variant with a more polar N-terminus, mutant F10E/L12E, because Thermus thermophilus ProDH (TtProDH), produced through fusion with maltose-binding protein (MBP) appears to be prone to aggregation. Preparation of TtProDH mutant variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, the mutant shows no electron density for an AMP moiety of the cofactor
F10E/L12E
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
construction of a variant with a more polar N-terminus, mutant F10E/L12E, because Thermus thermophilus ProDH (TtProDH), produced through fusion with maltose-binding protein (MBP) appears to be prone to aggregation. Preparation of TtProDH mutant variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, the mutant shows no electron density for an AMP moiety of the cofactor
-
generation of an enzyme-deficient prodh1 mutant
additional information
-
generation of an enzyme-deficient prodh1 mutant
additional information
-
truncated enzyme containing residues 86-601 and only four Trp residues. Substantial conformational changes of truncated protein upon addition of proline
additional information
expression of PRODH/POX in DLD-1 colorectal cancer cells significantly decreases basal and maximal respiration at both 3 and 5 days, and proline addition exacerbates this effect. PRODH/POX-dependent inhibition of respiration can be modulated by the duration of PRODH/POX expression and the availability of proline
additional information
the truncated form of Pseudomonas putida PutA shows proline dehydrogenase activity
additional information
-
the truncated form of Pseudomonas putida PutA shows proline dehydrogenase activity
additional information
-
the truncated form of Pseudomonas putida PutA shows proline dehydrogenase activity
-