4.3.1.15: Diaminopropionate ammonia-lyase
This is an abbreviated version!
For detailed information about Diaminopropionate ammonia-lyase, go to the full flat file.
Word Map on EC 4.3.1.15
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4.3.1.15
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typhimurium
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5'-phosphate
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plp-dependent
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alpha,beta-elimination
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d-isomer
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l-2,3-diaminopropionate
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monoclinic
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l-forms
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monovalent
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etch
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pseudomonad
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tetragonal
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neurotoxins
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dehydratase
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d-serine
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medicine
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analysis
- 4.3.1.15
- typhimurium
- 5'-phosphate
-
plp-dependent
-
alpha,beta-elimination
-
d-isomer
- l-2,3-diaminopropionate
-
monoclinic
-
l-forms
-
monovalent
-
etch
-
pseudomonad
-
tetragonal
-
neurotoxins
- dehydratase
- d-serine
- medicine
- analysis
Reaction
Synonyms
2,3-Diaminopropionate:ammonia-lyase, alpha,beta-Diaminopropionate ammonia-lyase, ammonia-lyase, diaminopropionate, DAP ammonia-lyase, DAPAL, Diaminopropionatase, diaminopropionate ammonia lyase, diaminopropionate ammonia-lyase, DpaL, EcDAPAL, L-Diaminopropionate ammonia-lyase, sDAPAL, STM1002, ygeX
ECTree
4.3.1.15 Diaminopropionate ammonia-lyaseAdvanced search results
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results (Engineering
Engineering on EC 4.3.1.15 - Diaminopropionate ammonia-lyase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C265S
Tm-value of the mutant enzyme is 60°C, compared to 65°C for the wild-type enzyme. The activity of the C291S mutant is higher than that of C265S mutant
C291S
Tm-value of the mutant enzyme is 68°C, compared to 65°C for the wild-type enzyme. The activity of the C291S mutant is higher than that of C265S mutant
D120N
mutant shows no reaction with D-DAP, Km (L-DAP) increased compared to wild-type, kcat decreased
D189N
Km (D-DAP) and (L-DAP) increased compared to wild-type, kcat decreased
C271V
C299V
D125E
mutant does not show any activity with D-DAP at all
D125S
kcat value in mutant is reduced by 5.4fold for D-DAP compared to wild-type
D194P
mutant does not show any activity with either L-DAP or D-DAP. Kd for D-DAP shows a 5fold increase in mutant compared to wild-type. L-DAP does not bind at all to mutant D194P
D194S
mutant exhibits an 16fold decrease in kcat with L-DAP whereas activity with D-DAP is reduced only by factor 1.7 compared to wild-type
T385D
kcat value with DL-DAP as substrate is 69% of wild-type. Km value for D-Ser doubled in T385D mutant whereas the kcat value increased by 7fold
T385S
kcat value with DL-DAP as substrate is 86% of wild-type. Mutant exhibits a 2fold higher Kcat with D-Ser compared to wild-type
C271V
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mutation results in a 47fold increase in Km and 1.5fold reduction in Kcat with respect to the wild type enzyme when DL-2,3-diaminopropanoate is used as substrate
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C299V
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mutation does not effect the activity
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C271V
Km for DL-DAP is 47fold higher compared to wild-type and kcat decreased by 1.5fold compared to wild-type.In contrast to wild-type C271V sDAPAL exhibits only 2fold stimulation in activity even when a high concentration of KCl is used
C271V
mutation results in a 47fold increase in Km and 1.5fold reduction in Kcat with respect to the wild type enzyme when DL-2,3-diaminopropanoate is used as substrate
C299V
kcat and Km for DL-DAP are similar to wild-type
C299V
mutation does not effect the activity
