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4.1.2.49 |
Description |
L-allo-threonine aldolase |
Alternative names |
L-allo-threonine acetaldehyde-lyase (glycine-forming) |
Catalyzed reaction |
L-allo-threonine = glycine + acetaldehyde |
Cofactor |
Pyridoxal-phosphate. |
Comments |
Requires pyridoxal phosphate. This enzyme, characterized from the bacterium Aeromonas jandaei, is specific for L-allo-threonine and can not act on either L-threonine or L-serine. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase. A previously listed enzyme with this name, EC 4.1.2.6, was deleted in 1971 after it was found to be identical to EC 2.1.2.1, glycine hydroxymethyltransferase.
Enzymes with this activity have been included in family 4.1.2.5 (threonine aldolase). |
Organisms |
-Eubacteria |
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Links |
Enzyme (activities) 4.1.2.49
BRENDA (activities) 4.1.2.49
KEGG (pathways) 4.1.2.49
PLPMDB (PLP mutants) 4.1.2.49
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References |
Articles on 4.1.2.49 |
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last changed |
2019/06/20 13:26 |
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