4.1.2.42: D-threonine aldolase
This is an abbreviated version!
For detailed information about D-threonine aldolase, go to the full flat file.
Word Map on EC 4.1.2.42
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4.1.2.42
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synthesis
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arthrobacter
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5'-phosphate
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alcaligenes
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xylosoxidans
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d-specific
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pharmacology
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low-specificity
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aldolases
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medicine
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reinhardtii
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dehydratase
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alpha-position
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plp-dependent
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beta-position
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pyridoxal-p
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erythro
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chlamydomonas
-
l-threonine
- 4.1.2.42
- synthesis
- arthrobacter
- 5'-phosphate
- alcaligenes
- xylosoxidans
-
d-specific
- pharmacology
-
low-specificity
- aldolases
- medicine
- reinhardtii
- dehydratase
-
alpha-position
-
plp-dependent
-
beta-position
-
pyridoxal-p
-
erythro
-
chlamydomonas
- l-threonine
Reaction
Synonyms
ARDTA, AXDTA, CrDTA, D-TA, D-threonine aldolase, DTA, low specificity D-TA, low specificity D-threonine aldolase
ECTree
4.1.2.42 D-threonine aldolaseAdvanced search results
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results (General Stability
General Stability on EC 4.1.2.42 - D-threonine aldolase
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GENERAL STABILITY 
ORGANISM
UNIPROT
LITERATURE
divalent transition metal cations (cobalt and nickel) improve the stability significantly. Ni2+ is the best and retains almost all activity on storage at 4 °C for a week. Although MnCl2 was required to catalyze the condensation
existence of the metal ions (Mn2+) enhances the stability of the enzyme
divalent transition metal cations (cobalt and nickel) improve the stability significantly. Ni2+ is the best and retains almost all activity on storage at 4 °C for a week. Although MnCl2 was required to catalyze the condensation
divalent transition metal cations (cobalt and nickel) improve the stability significantly. Ni2+ is the best and retains almost all activity on storage at 4 °C for a week. Although MnCl2 was required to catalyze the condensation
