1.1.1.108: carnitine 3-dehydrogenase
This is an abbreviated version!
For detailed information about carnitine 3-dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.108
-
1.1.1.108
-
hernia
-
diaphragmatic
-
prenatal
-
fetuses
-
survivors
-
anomalies
-
extracorporeal
-
neurodevelopmental
-
multicenter
-
xanthomonas
-
circumference
-
herniation
-
antenatal
-
translucens
-
trimethylamine
-
single-institution
-
alanine-scanning
-
between-run
-
synthesis
-
analysis
-
diagnostics
- 1.1.1.108
-
hernia
-
diaphragmatic
-
prenatal
-
fetuses
-
survivors
- anomalies
-
extracorporeal
-
neurodevelopmental
-
multicenter
-
xanthomonas
-
circumference
-
herniation
-
antenatal
- translucens
- trimethylamine
-
single-institution
-
alanine-scanning
-
between-run
- synthesis
- analysis
- diagnostics
Reaction
Synonyms
Cdh, CDHA, CDHB, CDHC, CDHR, L-(-)-carnitine dehydrogenase, L-carnitine dehydrogenase, L-CDH
ECTree
Advanced search results
Engineering
Engineering on EC 1.1.1.108 - carnitine 3-dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
S220G/F221A
-
the mutant shows reduced activity compared to the wild type enzyme
E185A
-
the mutant shows reduced activity compared to the wild type enzyme
E201A
-
the mutant shows reduced activity compared to the wild type enzyme
F143A
-
the mutant shows reduced activity compared to the wild type enzyme
F143C
-
the mutant shows reduced activity compared to the wild type enzyme
F143G
-
the mutant shows reduced activity compared to the wild type enzyme
F143H
-
the mutant shows reduced activity compared to the wild type enzyme
F143K
-
the mutant shows reduced activity compared to the wild type enzyme
F143N
-
the mutant shows reduced activity compared to the wild type enzyme
F143S
-
the mutant shows reduced activity compared to the wild type enzyme
F143Y
-
the mutant shows reduced activity compared to the wild type enzyme
F189A
-
the mutant shows reduced activity compared to the wild type enzyme
F234A
-
the mutant shows reduced activity compared to the wild type enzyme
G188A
-
the mutant shows reduced activity compared to the wild type enzyme
G233S/A224F
-
the mutant shows reduced activity compared to the wild type enzyme
I190V/A191G
-
the mutant shows reduced activity compared to the wild type enzyme
M231A
-
the mutant shows reduced activity compared to the wild type enzyme
M246A
-
the mutant shows reduced activity compared to the wild type enzyme
N144A
-
the mutant shows reduced activity compared to the wild type enzyme
Q252A
-
the mutant shows reduced activity compared to the wild type enzyme
R200A
-
the mutant shows reduced activity compared to the wild type enzyme
R297A
-
the mutant shows reduced activity compared to the wild type enzyme
S117A
-
the mutant shows reduced activity compared to the wild type enzyme
S120A
-
the mutant shows reduced activity compared to the wild type enzyme
T262A
-
the mutant shows reduced activity compared to the wild type enzyme
W228A
-
the mutant shows reduced activity compared to the wild type enzyme
Y147A
-
the mutant shows reduced activity compared to the wild type enzyme
Y237A
-
the mutant shows reduced activity compared to the wild type enzyme
additional information
-
strain PA14 mutants with transposon insertions in PA5385 and PA5388 result in the inability of Pseudomonas aeruginosa to grow on carnitine, mutants from the PAO1 transposon insertions in each of the PA5388, PA5387, PA5386 and PA5388 genes are unable to grow on carnitine
additional information
strain PA14 mutants with transposon insertions in PA5385 and PA5388 result in the inability of Pseudomonas aeruginosa to grow on carnitine, mutants from the PAO1 transposon insertions in each of the PA5388, PA5387, PA5386 and PA5388 genes are unable to grow on carnitine
additional information
deletion of the C-terminal thioesterase domain, mutant DELTA162-CDH, only slightly affects enzymic activity. Activity is eliminated by deletion of the whole C-terminal extra sequence in mutants DELTA168-CDH, DELTA174-CDH, DELTA178-CDH
additional information
-
deletion of the C-terminal 5-residue domain abolishes catalytic activity
additional information
-
deletion of the C-terminal 5-residue domain abolishes catalytic activity
-