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4.1.2.17: L-fuculose-phosphate aldolase

This is an abbreviated version!
For detailed information about L-fuculose-phosphate aldolase, go to the full flat file.

Word Map on EC 4.1.2.17

Reaction

L-Fuculose 1-phosphate
=
glycerone phosphate
 +
(S)-lactaldehyde

Synonyms

aldolase, L-fuculose phosphate, F-1PA, Fuc-1PA, FucA, fuculose aldolase, fuculose-1-phosphate aldolase, L-Fuc1P aldolase, L-Fuculose 1-phosphate aldolase, L-Fuculose phosphate aldolase, L-Fuculose-1-P aldolase, L-fuculose-1-phosphate aldolase, L-fuculose-phosphate aldolase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.17 L-fuculose-phosphate aldolase

Inhibitors

Inhibitors on EC 4.1.2.17 - L-fuculose-phosphate aldolase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-Cbz-alaninal
-
non-competitive inhibition
1,4-dideoxy-1,4-imino-L-arabinitol
-
-
1,4-dideoxy-1,4-iminod-arabinitol
-
-
D-fagomine
-
-
D-psicose 1-phosphate
product inhibition is noncompetitive vs. dihydroxyacetone phosphate and competitive vs. DL-glyceraldehyde. Product inhibition is uncompetitive against DHAP at saturated DL-glyceraldehyde
diethyldicarbonate
-
inactivates at 5 mM, rate is dependent on pH, glycerone phosphate protects
dihydroxyacetone phosphate
-
DL-threose
competitive with respect to dihydroxyacetone phosphate and uncompetitive with respect to DL-glyceraldehyde; the dead-end inhibition patterns as assessed by varying the concentration of dihydroxyacetone phosphate at several fixed concentrations of DL-threose is uncompetitive against dihydroxyacetone phosphate at the DL-glyceraldehyde Km concentration, and the dead-end inhibition by varying the concentrations of DL-threose is competitive against DL-glyceraldehyde at the DHAP Km concentration
L-fagomine
-
-
L-Tagatose 1-phosphate
product inhibition is noncompetitive vs. dihydroxyacetone phosphate and competitive vs. DL-glyceraldehyde. Product inhibition is uncompetitive against DHAP at saturated DL-glyceraldehyde
methylglyoxal
-
competitive inhibition
Phosphoglycolohydroxamate
-
-
trimethyl phosphonoacetate
competitive with respect to dihydroxyacetone phosphate and uncompetitive with respect to DL-glyceraldehyde; dead-end inhibition as assessed by varying the dihydroxyacetone phosphate concentration at several fixed concentrations of trimethyl phosphonoacetat: in the direction of the aldol addition reaction, trimethyl phosphonoacetate is competitive vs. dihydroxyacetone phosphate at the DL-glyceraldehyde Km concentration (0.74 mM). In the direction of the aldol addition reaction, trimethyl phosphonoacetate is competitive vs. DL-glyceraldehyde at the dihydroxyacetone phosphate Km concentration (0.091 mM). The dead-end inhibition patterns as assessed by varying the concentration of DL-glyceraldehyde at several fixed concentrations of trimethyl phosphonoacetate: in the direction of the aldol addition reaction, trimethyl phosphonoacetate is competitive vs. DL-glyceraldehyde at the dihydroxyacetone phosphate Km concentration
Zn2+
-
inhibitory effect of Zn2+ on his-tagged enzyme, but not on the native enzyme