4.1.2.48: low-specificity L-threonine aldolase
This is an abbreviated version!
For detailed information about low-specificity L-threonine aldolase, go to the full flat file.
Word Map on EC 4.1.2.48
Reaction
Synonyms
GLY1, GlyA, L-TA, L-threonine aldolase, low specificity L-TA, low specificity threonine aldolase, Low-specificity L-threonine aldolase, LTA, LtaE, serine hydroxy-methyl transferase, SHMT, threonine aldolase
ECTree
4.1.2.48 low-specificity L-threonine aldolaseAdvanced search results
results (
results (General Information
General Information on EC 4.1.2.48 - low-specificity L-threonine aldolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
knockout of the ltaE gene of wild-type Escherichia coli does not affect the cellular growth rate, while disruption of the ltaE gene of Escherichia coli GS245, whose serine hydroxymethyltransferase gene is knocked out, causes a significant decrease in the cellular growth rate, suggesting that the threonine aldolase is not a major source of cellular glycine in wild-type Escherichia coli but catalyzes an alternative pathway for cellular glycine when serine hydroxymethyltransferase is inert
metabolism
-
reversible cleavage of L-3-hydroxy-alpha-amino acids to glycine and the corresponding aldehydes
physiological function
physiological function
-
low-specificity L-threonine aldolase is involved in a serendipitous pathway that converts 3-phosphohydroxypyruvate, an intermediate in the serine biosynthesis pathway, to L-4-phosphohydroxythreonine, an intermediate in the pyridoxal-5'-phosphate synthesis pathway in a strain of Escherichia coli that lacks 4-phosphoerythronate dehydrogenase
physiological function
threonine aldolase is not a major source of cellular glycine in wild-type Escherichia coli but catalyzes an alternative pathway for cellular glycine when serine hydroxymethyltransferase is inert
