Any feedback?
Information on EC 4.1.2.17 - L-fuculose-phosphate aldolase
for references in articles please use BRENDA:EC4.1.2.17Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.1.2.17 L-fuculose-phosphate aldolaseSpecify your search results
Word Map
- 4.1.2.17
- dihydroxyacetone
- aldolases
- dhap
- l-rhamnulose-1-phosphate
- l-lactaldehyde
-
l-ribulose-5-phosphate
-
epimerase
- fucose
-
dhap-dependent
- iminocyclitols
-
epimer
-
epimerization
- l-1,2-propanediol
-
propanediol
-
polyhydroxylated
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
l-fuculose-1-phosphate aldolase, fuculose-1-phosphate aldolase, l-fuculose 1-phosphate aldolase, l-fuculose-phosphate aldolase, fuc-1pa, l-fuculose phosphate aldolase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldolase, L-fuculose phosphate
-
-
-
-
Fuc-1PA
-
-
-
-
FucA
fuculose aldolase
fuculose-1-phosphate aldolase
L-Fuculose 1-phosphate aldolase
-
-
-
-
L-Fuculose phosphate aldolase
-
-
-
-
L-Fuculose-1-P aldolase
-
-
-
-
L-fuculose-1-phosphate aldolase
L-fuculose-1-phosphate aldolase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-Fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
elimination
-
-
of an aldehyde, C-C bond cleavage
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9024-54-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2R)-2,3-dihydroxy-4-nitrobutanal
(1S,2R,3R,4R,5R,6R)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3,4,5-pentol + (1R,2R,3R,4R,5S,6S)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3,4,5-pentol
-
-
-
?
(2S)-2,3-dihydroxy-4-nitrobutanal
(1R,2R,3R,4S,5S,6S)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3,4,5-pentol + (1S,2R,3S,4S,5R,6R)-1-(hydroxymethyl)-6-nitrocyclohexane-1,2,3,4,5-pentol
-
-
-
?
(S)-Cbz-alaninal + dihydroxyacetone phosphate
(3R,4R,5S)-5-(benzyloxycarbonylamino)-5,6-dideoxy-1-phosphonohex-2-ulose
-
-
-
-
?
3-hydroxy-4-nitrobutanal
(1S,2R,3R,5S,6R)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3,5-tetraol + (1R,2R,3R,5R,6S)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3,5-tetraol
-
-
-
?
4-nitrobutanal
(1R,2R,3S,6S)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3-triol + (1S,2R,3R,6R)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3-triol
-
-
-
?
6-Deoxy-L-sorbose 1-phosphate
?
-
about 5% of the activity with L-fuculose 1-phosphate
-
-
?
D-Fructose 1,6-diphosphate
?
-
about 4% of the activity with L-fuculose 1-phosphate
-
-
?
D-Fructose 1-phosphate
?
-
about 4% of the activity with L-fuculose 1-phosphate
-
-
?
D-Ribulose 1,5-diphosphate
?
-
about 6% of the activity with L-fuculose 1-phosphate
-
-
?
dihydroxyacetone + (R)-N-benzyloxycarbonyl-alaninal
5-[[(benzyloxy)carbonyl]amino]-5,6-dideoxy-1-O-phosphonato-D-erythro-hex-2-ulose
-
-
-
-
?
dihydroxyacetone + (S)-N-benzyloxycarbonyl-alaninal
5-[[(benzyloxy)carbonyl]amino]-5,6-dideoxy-1-O-phosphonato-D-erythro-hex-2-ulose
-
-
-
-
?
dihydroxyacetone + benzyl (2R)-2-formylpyrrolidine-1-carboxylate
(3R,4R)-4-[1-[(benzyloxy)carbonyl]pyrrolidin-2-yl]-3,4-dihydroxy-2-oxobutyl phosphate
-
-
-
-
?
dihydroxyacetone + benzyl (2S)-2-formylpyrrolidine-1-carboxylate
(3R,4S)-4-[1-[(benzyloxy)carbonyl]pyrrolidin-2-yl]-3,4-dihydroxy-2-oxobutyl phosphate
-
-
-
-
?
dihydroxyacetone + benzyl [(2R)-3-methyl-1-oxobutan-2-yl]carbamate
(3R,4R,5R)-5-[[(benzyloxy)carbonyl]amino]-3,4-dihydroxy-6-methyl-2-oxoheptyl phosphate
-
-
-
-
?
dihydroxyacetone + benzyl [(2R)-4-methyl-1-oxopentan-2-yl]carbamate
(3R,4R,5R)-5-[[(benzyloxy)carbonyl]amino]-3,4-dihydroxy-7-methyl-2-oxooctyl phosphate
-
-
-
-
?
dihydroxyacetone + benzyl [(2S)-3-methyl-1-oxobutan-2-yl]carbamate
(3R,4R,5R)-5-[[(benzyloxy)carbonyl]amino]-3,4-dihydroxy-6-methyl-2-oxoheptyl phosphate + (3R,4S,5R)-5-[[(benzyloxy)carbonyl]amino]-3,4-dihydroxy-6-methyl-2-oxoheptyl phosphate
-
-
70:30 product ratio
-
?
dihydroxyacetone + benzyl [(2S)-4-methyl-1-oxopentan-2-yl]carbamate
(3R,4R,5R)-5-[[(benzyloxy)carbonyl]amino]-3,4-dihydroxy-7-methyl-2-oxooctyl phosphate
-
-
-
-
?
dihydroxyacetone + benzyl [(3S)-3-methyl-1-oxopentan-2-yl]carbamate
(3R,4R,5R,6S)-5-(((benzyloxy)carbonyl)amino)-3,4-dihydroxy-6-methyl-2-oxooctyl phosphate + (3R,4S,5R,6S)-5-(((benzyloxy)carbonyl)amino)-3,4-dihydroxy-6-methyl-2-oxooctyl phosphate
-
-
78:22 product ratio
-
?
dihydroxyacetone phosphate + L-lactaldehyde
L-fuculose 1-phosphate
-
-
-
-
r
dihydroxyacetone phosphate + N-Cbz-(2R)-2-amino-3-methylbutanal
N-Cbz-5-amino-1,3,4-trihydroxyoctan-2-one
-
wild-type 65% aldol adduct formed, mutant F131A, 76% aldol adduct formed
-
-
?
dihydroxyacetone phosphate + N-Cbz-(2R)-2-amino-4-methylpentanal
N-Cbz-5-amino-1,3,4-trihydroxy-7-methyloctan-2-one
-
-
-
-
?
dihydroxyacetone phosphate + N-Cbz-(2S)-2-amino-3-methylbutanal
N-Cbz-5-amino-1,3,4-trihydroxyoctan-2-one
-
wild-type 48% aldol adduct formed, mutant F131A, 60% aldol adduct formed
-
-
?
dihydroxyacetone phosphate + N-Cbz-(2S)-2-aminopropanal
N-Cbz-5-amino-1,3,4-trihydroxyhexan-2-one
-
wild-type 65% aldol adduct formed, mutant F131A, 64% aldol adduct formed
-
-
?
dihydroxyacetone phosphate + N-Cbz-aminoacetaldehyde
N-Cbz-5-amino-1,3,4-trihydroxypentan-2-one
-
wild-type 63% aldol adduct formed, mutant F131A, 50% aldol adduct formed
-
-
?
dimethoxyacetaldehyde + glycerone phosphate
(3R,4S)-3,4-dihydroxy-5,5-dimethoxy-2-oxopentyl phosphate
-
-
-
?
DL-glycerol 3-phosphate + DL-glyceraldehyde
D-psicose 1-phosphate
-
-
-
r
glycerone phosphate + L-glyceraldehyde
L-fructose 1-phosphate
-
-
-
?
L-glycerol 3-phosphate + D-glyceraldehyde
D-psicose 1-phosphate
-
L-glycerol 3-phosphate i.e. dihydroxyacetone phosphate, i.e. glycerone-3-phosphate
-
-
?
L-glycerol 3-phosphate + glycoaldehyde
D-ribulose 1-phosphate
-
L-glycerol 3-phosphate i.e. dihydroxyacetone phosphate, i.e. glycerone-3-phosphate
-
-
?
L-glycerol 3-phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
-
L-glycerol 3-phosphate i.e. dihydroxyacetone phosphate, i.e. glycerone-3-phosphate
-
-
?
dihydroxyacetone phosphate + D-glyceraldehyde
D-psicose 1-phosphate
kinetic mechanism is sequential, ordered addition of dihydroxyacetone phosphate prior to D-glyceraldehyde
-
-
?
dihydroxyacetone phosphate + D-glyceraldehyde
D-psicose 1-phosphate
kinetic mechanism is sequential, ordered addition of dihydroxyacetone phosphate prior to D-glyceraldehyde
-
-
?
dihydroxyacetone phosphate + DL-glyceraldehyde
L-tagatose 1-phosphate
-
-
-
r
dihydroxyacetone phosphate + DL-glyceraldehyde
L-tagatose 1-phosphate
-
-
-
r
dihydroxyacetone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
kinetic mechanism is sequential, ordered addition of dihydroxyacetone phosphate prior to L-glyceraldehyde
-
-
?
dihydroxyacetone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
kinetic mechanism is sequential, ordered addition of dihydroxyacetone phosphate prior to L-glyceraldehyde
-
-
?
dihydroxyacetone phosphate + L-lactaldehyde
L-fuculose-1-phosphate
-
-
-
r
dihydroxyacetone phosphate + L-lactaldehyde
L-fuculose-1-phosphate
-
-
-
r
DL-glycerol 3-phosphate + D-glyceraldehyde
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
DL-glycerol 3-phosphate + dihydroxyacetone phosphate
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
Glycerone phosphate + (R)-lactaldehyde
6-Deoxy-D-psicose 1-phosphate
-
at 73% of the activity with (S)-lactaldehyde
-
-
?
Glycerone phosphate + (R)-lactaldehyde
6-Deoxy-D-psicose 1-phosphate
-
at 73% of the activity with (S)-lactaldehyde
-
?
Glycerone phosphate + (R)-lactaldehyde
6-Deoxy-D-psicose 1-phosphate
-
at 73% of the activity with (S)-lactaldehyde
-
-
?
Glycerone phosphate + (R)-lactaldehyde
6-Deoxy-D-psicose 1-phosphate
-
at 73% of the activity with (S)-lactaldehyde
-
?
Glycerone phosphate + (S)-lactaldehyde
L-Fuculose 1-phosphate
-
-
-
?
Glycerone phosphate + (S)-lactaldehyde
L-Fuculose 1-phosphate
-
-
-
?
glycerone phosphate + D-glyceraldehyde
D-psicose 1-phosphate
-
at 33% of the activity with (S)-lactaldehyde
-
-
?
glycerone phosphate + D-glyceraldehyde
D-psicose 1-phosphate
-
at 33% of the activity with (S)-lactaldehyde
-
?
glycerone phosphate + D-glyceraldehyde
D-psicose 1-phosphate
-
at 33% of the activity with (S)-lactaldehyde
-
-
?
glycerone phosphate + D-glyceraldehyde
D-psicose 1-phosphate
-
at 33% of the activity with (S)-lactaldehyde
-
?
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
-
at 10% of the activity with (S)-lactaldehyde
-
-
?
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
-
at 10% of the activity with (S)-lactaldehyde
-
?
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
-
at 10% of the activity with (S)-lactaldehyde
-
-
?
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
-
at 10% of the activity with (S)-lactaldehyde
-
?
glycerone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
-
-
-
?
glycerone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
-
at 33% of the activity with (S)-lactaldehyde
-
-
?
glycerone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
-
at 33% of the activity with (S)-lactaldehyde
-
?
glycerone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
-
at 33% of the activity with (S)-lactaldehyde
-
?
L-fuculose 1-phosphate
dihydroxyacetone phosphate + (S)-lactaldehyde
-
-
-
-
?
L-fuculose 1-phosphate
dihydroxyacetone phosphate + (S)-lactaldehyde
-
-
-
-
?
L-fuculose 1-phosphate
dihydroxyacetone phosphate + (S)-lactaldehyde
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
r
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
r
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
-
r
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
-
r
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
r
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
r
L-glycerol 3-phosphate + D-glyceraldehyde
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
additional information
?
-
-
(R)-N-benzyloxycarbonyl-prolinal is not a substrate for the wild type enzyme
-
-
?
additional information
?
-
rapid equilibrium ordered mechanism in which dihydroxyacetone phosphate is added and bound to the enzyme prior to DL-glyceraldehyde
-
-
?
additional information
?
-
-
rapid equilibrium ordered mechanism in which dihydroxyacetone phosphate is added and bound to the enzyme prior to DL-glyceraldehyde
-
-
?
additional information
?
-
rapid equilibrium ordered mechanism in which dihydroxyacetone phosphate is added and bound to the enzyme prior to DL-glyceraldehyde
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dihydroxyacetone phosphate + L-lactaldehyde
L-fuculose 1-phosphate
-
-
-
-
r
Glycerone phosphate + (S)-lactaldehyde
L-Fuculose 1-phosphate
-
-
-
?
L-fuculose 1-phosphate
dihydroxyacetone phosphate + (S)-lactaldehyde
-
-
-
-
?
L-fuculose 1-phosphate
dihydroxyacetone phosphate + (S)-lactaldehyde
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
r
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
-
r
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
-
r
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
-
can substitute for the naturally occuring Zn2+, with somewhat higher activity
Mg2+
Mn2+
Zn2+
additional information
additional information
no zinc atom is trapped in the active site of the apo structure, crystallization data
additional information
-
no zinc atom is trapped in the active site of the apo structure, crystallization data
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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-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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.743
D-glyceraldehyde
assay with DL-glyceraldehyde, pH and temperature not specified in the publication
0.743
L-glyceraldehyde
assay with DL-glyceraldehyde, pH and temperature not specified in the publication
additional information
additional information
-
for FucA catalysis, the rate of the aldol addition reaction of dihydroxyaceone phosphate to N-Cbz-amino aldehydes in borate is between 2 to 10 times faster than that inTEA buffer. Moreover, the yields of aldol adduct improve between 1.5 to 4-fold for both FucA wild-type and the F131A mutant
-
0.091
dihydroxyacetone phosphate
pH and temperature not specified in the publication
0.091
dihydroxyacetone phosphate
pH not specified in the publication, temperature not specified in the publication
0.743
DL-glyceraldehyde
pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19
L-Fuculose 1-phosphate
pH 7.5, 37°C, wild-type enzyme and E214A mutant