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IUBMB CommentsThe enzyme, characterized from the bacterium Pseudomonas putida, is involved in an L-lysine catabolic pathway. Contains Fe(II).
The expected taxonomic range for this enzyme is: Pseudomonas putida
Synonyms
pp_5260,
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PP_5260
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ydcJ
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2-oxoadipate + O2 = (R)-2-hydroxyglutarate + CO2
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2-oxoadipate dioxygenase/carboxy lyase
The enzyme, characterized from the bacterium Pseudomonas putida, is involved in an L-lysine catabolic pathway. Contains Fe(II).
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2-oxoadipate + O2
(R)-2-hydroxyglutarate + CO2
2-oxoadipate + O2
(R)-2-hydroxyglutarate + CO2
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?
2-oxoadipate + O2
(R)-2-hydroxyglutarate + CO2
-
-
-
?
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2-oxoadipate + O2
(R)-2-hydroxyglutarate + CO2
2-oxoadipate + O2
(R)-2-hydroxyglutarate + CO2
-
-
-
?
2-oxoadipate + O2
(R)-2-hydroxyglutarate + CO2
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?
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EDTA
complete loss of activity, only presence of Fe(II) restores activity
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0.06
2-oxoadipate
pH 7, 30°C
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5.5
2-oxoadipate
pH 7, 30°C
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UniProt
brenda
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UniProt
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evolution
member of the DUF1338 protein family
evolution
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member of the DUF1338 protein family
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physiological function
enzyme is involved in an L-lysine catabolic pathway. A gene deletion strain is unable to grow on either isomer of lysine
physiological function
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enzyme is involved in an L-lysine catabolic pathway. A gene deletion strain is unable to grow on either isomer of lysine
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Q88CC1_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
464
0
51372
TrEMBL
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Thompson, M.; Blake-Hedges, J.; Cruz-Morales, P.; Barajas, J.; Curran, S.; Eiben, C.; Harris, N.; Benites, V.; Gin, J.; Sharpless, W.; Twigg, F.; Skyrud, W.; Krishna, R.; Pereira, J.; Baidoo, E.; Petzold, C.; Adams, P.; Arkin, A.; Deutschbauer, A.; Keasling, J.D.
Massively parallel fitness profiling reveals multiple novel enzymes in Pseudomonas putida lysine metabolism
mBio
10
e02577-18
2019
Pseudomonas putida (Q88CC1), Pseudomonas putida, Pseudomonas putida DSM 6125 (Q88CC1)
brenda
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1.13.11.93 2-oxoadipate dioxygenase/decarboxylase
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