4.3.1.2: methylaspartate ammonia-lyase
This is an abbreviated version!
For detailed information about methylaspartate ammonia-lyase, go to the full flat file.
Word Map on EC 4.3.1.2
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4.3.1.2
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seizure
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grand
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epilepsy
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petit
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children
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convulsion
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pain
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discharge
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anticonvulsant
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photodynamic
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myoclonic
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woman
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electroencephalograph
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allergen
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aminolevulinate
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antiepileptic
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wave
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awaken
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palmoplantar
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diazepam
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phenytoin
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tonic-clonic
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arcuate
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celiac
-
cream
-
rehabilitation
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hemiparesis
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consciousness
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carbamazepine
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ligament
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paroxysm
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birch
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epilepticus
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seizure-free
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electroshock
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clonazepam
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jerk
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psychogenic
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analysis
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reoviridae
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ictal
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keratoses
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trif
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maackia
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amurensis
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interictal
-
clonic
-
synthesis
-
biotechnology
-
diphenylhydantoin
-
sway
-
daylight
-
wolf
- 4.3.1.2
- seizure
-
grand
- epilepsy
-
petit
- children
- convulsion
- pain
- discharge
-
anticonvulsant
-
photodynamic
-
myoclonic
- woman
-
electroencephalograph
- allergen
-
aminolevulinate
-
antiepileptic
-
wave
-
awaken
-
palmoplantar
- diazepam
- phenytoin
-
tonic-clonic
-
arcuate
-
celiac
-
cream
-
rehabilitation
- hemiparesis
- consciousness
- carbamazepine
-
ligament
-
paroxysm
- birch
- epilepticus
-
seizure-free
-
electroshock
- clonazepam
- jerk
-
psychogenic
- analysis
- reoviridae
-
ictal
- keratoses
- trif
-
maackia
- amurensis
-
interictal
-
clonic
- synthesis
- biotechnology
- diphenylhydantoin
-
sway
-
daylight
- wolf
Reaction
Synonyms
3-methyl-L-aspartic acid ammonia-lyase, 3-methylaspartase, 3-methylaspartate ammonia lyase, 3-methylaspartate ammonia-lyase, ammonia-lyase, methylaspartate, beta-methylaspartase, Ch-MAL, MAL, methylaspartate ammonia lyase, methylaspartate ammonia-lyase, threo-3-methyl-L-aspartate ammonia-lyase, threo-3-methylaspartase ammonia-lyase
ECTree
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Engineering
Engineering on EC 4.3.1.2 - methylaspartate ammonia-lyase
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C361A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 47% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
C361K
mutant shows no reactivity. Conversion 2h: 10% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
F170A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 63% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
L384A
Q172A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 16% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
Q172N
mutant shows no reactivity. Conversion 2h: 6% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
Q73A
Q73N
mutant shows very low-level amination activity preventing the measurement of kinetic parameters. Conversion 2h: 18% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
T360A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 38% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 93:7 (89:11 wild-type)
T360S
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 76% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 86:14 (89:11 wild-type)
Y356A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 24% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 61% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)
L384A
mutant displays pronounced amination activity towards 2-hexylfumarate ad decreased amination activity towards mesaconate compared to wild-type. Mutant displays a broad electrophile scope including fumarate derivatives with alkyl, aryl, alkoxy, aryloxy, alkylthio and arylthio substituents at the C2 position
analysis carried out with mutant Q73A. The potential of the mutant Q73A enzyme is shown for application in the asymmetric synthesis of a large variety of valuable N-substituted l-aspartic acids
Q73A
kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 37% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 91:9 (89:11 wild-type)
Q73A
mutant displays significant decrease in ammonia addition and a large increase in methylamine addition compared to wild-type. Mutant displays a wide nucleophile scope including structurally diverse linear and cyclic allkylamines