Literature summary for 4.1.2.13 extracted from

Gutierrez, M.; Parella, T.; Joglar, J.; Bujons J.; Clap�s P.
Structure-guided redesign of D-fructose-6-phosphate aldolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutation (2011), Chem. Commun. (Camb. ), 47, 5762-5764.

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Protein Variants

Protein Variants	Comment	Organism
A129S/A165G	activity is between 5- to more than 900fold higher than that of wild-type towards N-Cbz-aminoaldehyde derivatives	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
dihydroxyacetone + phenyl [(2R)-1-oxopropan-2-yl]carbamate	i.e. (S)-N-Cbz-alaninal,substrate only for mutant A129S/A165G	Escherichia coli	phenyl [(2R,3R,4S)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate	aldol adduct is a key intermediates for the expedient synthesis of the pyrrolidine type iminocyclitol, 2,5-imino-1,2,5-trideoxy-D-mannitol	?
dihydroxyacetone + phenyl [(2S)-1-oxopropan-2-yl]carbamate	i.e. (S)-N-Cbz-alaninal, substrate only for mutant A129S/A165G	Escherichia coli	phenyl [(2S,3R,4S)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate	aldol adduct is a key intermediates for the expedient synthesis of the pyrrolidine type iminocyclitol, 2,5-imino-1,2,5-trideoxy-D-glucitol	?
hydroxyacetone + phenoxyacetaldehyde	substrate only for mutant A129S/A165G	Escherichia coli	?	-	?
hydroxyacetone + phenyl (2-oxoethyl)carbamate	substrate only for mutant A129S/A165G	Escherichia coli	?	-	?
hydroxyacetone + phenyl (3-oxopropyl)carbamate	substrate only for mutant A129S/A165G	Escherichia coli	?	-	?
hydroxyacetone + phenyl [(2R)-1-oxopropan-2-yl]carbamate	substrate only for mutant A129S/A165G	Escherichia coli	phenyl [(2R,3R,4S)-3,4-dihydroxy-5-oxohexan-2-yl]carbamate	-	?
hydroxyacetone + phenyl [(2S)-1-oxopropan-2-yl]carbamate	substrate only for mutant A129S/A165G	Escherichia coli	phenyl [(2S,3R,4S)-3,4-dihydroxy-5-oxohexan-2-yl]carbamate	-	?

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Release 2023.1 (January 2023)