Information on EC 4.1.2.17 - L-fuculose-phosphate aldolase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY
4.1.2.17
-
RECOMMENDED NAME
GeneOntology No.
L-fuculose-phosphate aldolase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-Fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aldol addition
-
-
elimination
-
-
elimination
-
-
of an aldehyde, C-C bond cleavage
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
degradation of hexoses
-
-
degradation of pentoses
-
-
Fructose and mannose metabolism
-
-
fucose degradation
-
-
lactate biosynthesis (archaea)
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aldolase, L-fuculose phosphate
-
-
-
-
Fuc-1PA
-
-
-
-
fuculose-1-phosphate aldolase
-
-
fuculose-1-phosphate aldolase
-
-
fuculose-1-phosphate aldolase
Q58813
-
fuculose-1-phosphate aldolase
Q58813
-
-
L-Fuc1P 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
-
-
L-fuculose-1-phosphate aldolase
-
-
L-fuculose-phosphate aldolase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-54-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 0111-B4
-
-
Manually annotated by BRENDA team
Escherichia coli 0111-B4
strain 0111-B4
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
HB8, recombinant
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-Cbz-alaninal + dihydroxyacetone phosphate
(3R,4R,5S)-5-(benzyloxycarbonylamino)-5,6-dideoxy-1-phosphonohex-2-ulose
show the reaction diagram
-
-
-
-
?
6-Deoxy-L-sorbose 1-phosphate
?
show the reaction diagram
-
about 5% of the activity with L-fuculose 1-phosphate
-
-
-
D-Fructose 1,6-diphosphate
?
show the reaction diagram
-
about 4% of the activity with L-fuculose 1-phosphate
-
-
-
D-Fructose 1-phosphate
?
show the reaction diagram
-
about 4% of the activity with L-fuculose 1-phosphate
-
-
-
D-Ribulose 1,5-diphosphate
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
dihydroxyacetone + (S)-N-benzyloxycarbonyl-alaninal
5-[[(benzyloxy)carbonyl]amino]-5,6-dideoxy-1-O-phosphonato-D-erythro-hex-2-ulose
show the reaction diagram
-
-
-
-
?
dihydroxyacetone + benzyl (2R)-2-formylpyrrolidine-1-carboxylate
(3R,4R)-4-[1-[(benzyloxy)carbonyl]pyrrolidin-2-yl]-3,4-dihydroxy-2-oxobutyl phosphate
show the reaction diagram
-
-
-
-
?
dihydroxyacetone + benzyl (2S)-2-formylpyrrolidine-1-carboxylate
(3R,4S)-4-[1-[(benzyloxy)carbonyl]pyrrolidin-2-yl]-3,4-dihydroxy-2-oxobutyl phosphate
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
78:22 product ratio
-
?
dihydroxyacetone phosphate
methylglyoxal + phosphate
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + D-glyceraldehyde
D-psicose 1-phosphate
show the reaction diagram
Q58813
kinetic mechanism is sequential, ordered addition of dihydroxyacetone phosphate prior to D-glyceraldehyde
-
-
?
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
r
dihydroxyacetone phosphate + DL-glyceraldehyde
L-tagatose 1-phosphate
show the reaction diagram
Q58813
-
-
-
r
dihydroxyacetone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
show the reaction diagram
Q58813
kinetic mechanism is sequential, ordered addition of dihydroxyacetone phosphate prior to L-glyceraldehyde
-
-
?
dihydroxyacetone phosphate + L-lactaldehyde
L-fuculose 1-phosphate
show the reaction diagram
-
-
-
-
r
dihydroxyacetone phosphate + L-lactaldehyde
L-rhamnulose-1-phosphate
show the reaction diagram
-
-
-
-
r
dihydroxyacetone phosphate + L-lactaldehyde
L-fuculose-1-phosphate
show the reaction diagram
Q58813
-
-
-
r
dihydroxyacetone phosphate + N-Cbz-(2R)-2-amino-3-methylbutanal
N-Cbz-5-amino-1,3,4-trihydroxyoctan-2-one
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + N-Cbz-(2S)-2-amino-3-methylbutanal
N-Cbz-5-amino-1,3,4-trihydroxyoctan-2-one
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
wild-type 63% aldol adduct formed, mutant F131A, 50% aldol adduct formed
-
-
?
dihydroxyacetonphosphate + (S)-Cbz-alaninal
?
show the reaction diagram
-
-
-
-
?
DL-glycerol 3-phosphate + D-glyceraldehyde
?
show the reaction diagram
-
-
-
-
?
DL-glycerol 3-phosphate + dihydroxyacetone phosphate
?
show the reaction diagram
-
-
-
-
?
DL-glycerol 3-phosphate + DL-glyceraldehyde
D-psicose 1-phosphate
show the reaction diagram
Q58813
-
-
-
r
Glycerone phosphate + (R)-lactaldehyde
6-Deoxy-D-psicose 1-phosphate
show the reaction diagram
-
at 73% of the activity with (S)-lactaldehyde
-
-
-
Glycerone phosphate + (R)-lactaldehyde
6-Deoxy-D-psicose 1-phosphate
show the reaction diagram
-
at 73% of the activity with (S)-lactaldehyde
-
-
Glycerone phosphate + (R)-lactaldehyde
6-Deoxy-D-psicose 1-phosphate
show the reaction diagram
Escherichia coli 0111-B4
-
at 73% of the activity with (S)-lactaldehyde
-
-
-
Glycerone phosphate + (R)-lactaldehyde
6-Deoxy-D-psicose 1-phosphate
show the reaction diagram
Escherichia coli 0111-B4, Escherichia coli K12
-
at 73% of the activity with (S)-lactaldehyde
-
-
Glycerone phosphate + (S)-lactaldehyde
L-Fuculose 1-phosphate
show the reaction diagram
-
-
-
-
Glycerone phosphate + (S)-lactaldehyde
L-Fuculose 1-phosphate
show the reaction diagram
Escherichia coli, Escherichia coli 0111-B4
-
-
-
-
Glycerone phosphate + D-glyceraldehyde
D-Psicose 1-phosphate
show the reaction diagram
-
at 33% of the activity with (S)-lactaldehyde
-
-
-
Glycerone phosphate + D-glyceraldehyde
D-Psicose 1-phosphate
show the reaction diagram
-
at 33% of the activity with (S)-lactaldehyde
-
-
Glycerone phosphate + D-glyceraldehyde
D-Psicose 1-phosphate
show the reaction diagram
Escherichia coli 0111-B4
-
at 33% of the activity with (S)-lactaldehyde
-
-
-
Glycerone phosphate + D-glyceraldehyde
D-Psicose 1-phosphate
show the reaction diagram
Escherichia coli 0111-B4, Escherichia coli K12
-
at 33% of the activity with (S)-lactaldehyde
-
-
glycerone phosphate + DL-glyceraldehyde
?
show the reaction diagram
-
-
-
?
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
show the reaction diagram
-
at 10% of the activity with (S)-lactaldehyde
-
-
-
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
show the reaction diagram
-
at 10% of the activity with (S)-lactaldehyde
-
-
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
show the reaction diagram
Escherichia coli 0111-B4
-
at 10% of the activity with (S)-lactaldehyde
-
-
-
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
show the reaction diagram
Escherichia coli 0111-B4, Escherichia coli K12
-
at 10% of the activity with (S)-lactaldehyde
-
-
Glycerone phosphate + L-glyceraldehyde
L-Tagatose 1-phosphate
show the reaction diagram
-
at 33% of the activity with (S)-lactaldehyde
-
-
-
Glycerone phosphate + L-glyceraldehyde
L-Tagatose 1-phosphate
show the reaction diagram
Escherichia coli, Escherichia coli 0111-B4, Escherichia coli K12
-
at 33% of the activity with (S)-lactaldehyde
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
r
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
P0AB87
-
-
?
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
?
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
r
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
r
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
r
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
r
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
Escherichia coli 0111-B4
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
Escherichia coli 0111-B4
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
Escherichia coli K12
-
-
-
-
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
Escherichia coli K12
-
-
-
-
L-Fuculose 1-phosphate
?
show the reaction diagram
-
initial step in the metabolism of L-fucose
-
-
-
L-fuculose 1-phosphate
dihydroxyacetone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
?
L-fuculose 1-phosphate
dihydroxyacetone + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
?
L-glycerol 3-phosphate + D-glyceraldehyde
?
show the reaction diagram
-
-
-
-
?
L-glycerol 3-phosphate + D-glyceraldehyde
D-psicose 1-phosphate
show the reaction diagram
-
L-glycerol 3-phosphate i.e. dihydroxyacetone phosphate, i.e. glycerone-3-phosphate
-
-
?
L-glycerol 3-phosphate + glycoaldehyde
D-ribulose 1-phosphate
show the reaction diagram
-
L-glycerol 3-phosphate i.e. dihydroxyacetone phosphate, i.e. glycerone-3-phosphate
-
-
?
L-glycerol 3-phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
show the reaction diagram
-
L-glycerol 3-phosphate i.e. dihydroxyacetone phosphate, i.e. glycerone-3-phosphate
-
-
?
additional information
?
-
P0AB87
fucose metabolism
-
?
additional information
?
-
-
(R)-N-benzyloxycarbonyl-prolinal is not a substrate for the wild type enzyme
-
-
-
additional information
?
-
Q58813
rapid equilibrium ordered mechanism in which dihydroxyacetone phosphate is added and bound to the enzyme prior to DL-glyceraldehyde
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
r
dihydroxyacetone phosphate + L-lactaldehyde
L-fuculose 1-phosphate
show the reaction diagram
-
-
-
-
r
dihydroxyacetone phosphate + L-lactaldehyde
L-rhamnulose-1-phosphate
show the reaction diagram
-
-
-
-
r
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
r
L-Fuculose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
r
L-Fuculose 1-phosphate
?
show the reaction diagram
-
initial step in the metabolism of L-fucose
-
-
-
L-fuculose 1-phosphate
dihydroxyacetone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
?
additional information
?
-
P0AB87
fucose metabolism
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
0.01 M, restores activity after dialysis with EDTA; divalent cation required
Ca2+
-
divalent cation required
Co2+
-
can substitute for the naturally occuring Zn2+, with somewhat higher activity
Mg2+
-
0.01 M, restores activity after dialysis with EDTA; divalent cation required
Zn2+
-
contains tightly bound Zn2+
Zn2+
-
required
Zn2+
-
optimal concentration: 0.01 mM
Zn2+
Q58813
contains a catalytically active Zn2+ ion
Mn2+
-
0.01 M, restores activity after dialysis with EDTA; divalent cation required
additional information
Q5SHB9
no zinc atom is trapped in the active site of the apo structure, crystallization data
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
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
Q58813
; 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
Q58813
-
DL-glyceraldehyde
Q58813
-
DL-threose
Q58813
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
Q58813
; 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
Q58813
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.743
D-glyceraldehyde
Q58813
assay with DL-glyceraldehyde, pH and temperature not specified in the publication
0.091
dihydroxyacetone phosphate
Q58813
pH and temperature not specified in the publication; pH not specified in the publication, temperature not specified in the publication
54.7
dihydroxyacetone phosphate
-
-
0.743
DL-glyceraldehyde
Q58813
pH not specified in the publication, temperature not specified in the publication
7.8
DL-glyceraldehyde
-
wild-type
8.2
DL-glyceraldehyde
-
N25T mutant
23.1
DL-glyceraldehyde
-
N25L mutant
0.36
glycerone phosphate
-
N25L mutant
1.01
glycerone phosphate
-
wild-type
5
glycerone phosphate
-
N25T mutant
0.5
L-Fuculose 1-phosphate
-
pH 7.5, 37C, Y113F mutant
0.7
L-Fuculose 1-phosphate
-
-
1.8
L-Fuculose 1-phosphate
-
pH 7.5, 37C, R212A mutant
2
L-Fuculose 1-phosphate
-
pH 7.5, 37C, wild-type enzyme
2.2
L-Fuculose 1-phosphate
-
pH 7.5, 37C, wild-type
3
L-Fuculose 1-phosphate
-
pH 7.5, 37C, E214D mutant; pH 7.5, 37C, E215A mutant
4.4
L-Fuculose 1-phosphate
-
pH 7.5, 37C, Y209F mutant
6
L-Fuculose 1-phosphate
-
pH 7.5, 37C, E214Q and T26A mutant
7
L-Fuculose 1-phosphate
-
pH 7.5, 37C, K207A mutant
8
L-Fuculose 1-phosphate
-
pH 7.5, 37C, E214A mutant
11
L-Fuculose 1-phosphate
-
pH 7.5, 37C, F206W mutant
22
L-Fuculose 1-phosphate
-
pH 7.5, 37C, F131A mutant
74
L-Fuculose 1-phosphate
-
pH 7.5, 37C, E214L mutant
130
L-Fuculose 1-phosphate
-
pH 7.5, 37C, N29Q mutant
0.743
L-Glyceraldehyde
Q58813
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.36
dihydroxyacetone phosphate
-
-
19.3
dihydroxyacetone phosphate
-
-
0.4
L-Fuculose 1-phosphate
-
pH 7.5, 37C, Y113F mutant
0.6
L-Fuculose 1-phosphate
-
pH 7.5, 37C, F131A mutant
1.3
L-Fuculose 1-phosphate
-
pH 7.5, 37C, Y209F mutant
4
L-Fuculose 1-phosphate
-
pH 7.5, 37C, T26A mutant
5.5
L-Fuculose 1-phosphate
-
pH 7.5, 37C, N29Q mutant
8
L-Fuculose 1-phosphate
-
pH 7.5, 37C, F206W mutant
12
L-Fuculose 1-phosphate
-
pH 7.5, 37C, R212A mutant
13
L-Fuculose 1-phosphate
-
pH 7.5, 37C, E214L mutant
19
L-Fuculose 1-phosphate
-
pH 7.5, 37C, wild-type enzyme and E214A mutant
19
L-Fuculose 1-phosphate
-
pH 7.5, 37C, wild-type
20
L-Fuculose 1-phosphate
-
pH 7.5, 37C, E214D and K207A mutant
21
L-Fuculose 1-phosphate
-
pH 7.5, 37C, E214Q mutant
22
L-Fuculose 1-phosphate
-
pH 7.5, 37C, E215A mutant
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0123
dihydroxyacetone phosphate
Q58813
direction of aldol condensation, pH not specified in the publication, temperature not specified in the publication
0.01
DL-glyceraldehyde
Q58813
direction of aldol condensation, pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00055
-
H218N mutant
0.0011
-
D76E mutant
0.0012
-
D120N mutant
0.0013
-
K42M mutant
0.0061
-
N28A mutant
0.0063
-
H97N mutant
0.0085
-
wild-type
0.0122
-
E142Q mutant
0.0133
Q58813
in the direction of hydrolysis, pH and temperature not specified in the publication
0.0256
Q58813
in the direction of aldol condensation, pH and temperature not specified in the publication
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9 - 7.2
-
-
7.5
-
FucA activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
pH 6: about 30% of maximal activity, pH 10: about 35% of maximal activity
6.4 - 8.8
-
pH 6.4: about 30% of maximal activity, pH 8.8: about 40% of maximal activity
6.5 - 8
-
approximately 50% of maximal activity at pH 6.5 and at pH 8
6.5 - 8.2
-
approximately 50% of maximal activity at pH 6.5 and at pH 8.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
FucA activity assay
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
-
monomer
690787
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
Q5SHB9
crystallization data
homotetramer
-
-
tetramer
-
-
tetramer
-
4 * 23775, calculation from nucleotide sequence
tetramer
-
4 * 24000
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cocrystallized with phosphoglycolohydroxamate
-
hanging drop vapor diffusion method
-
sitting-drop vapour-diffusion and microbatch techniques. Crystals belong to space group P4, with unit-cell parameters a = b = 100.94 A, c = 45.87 A
-
to 1.9 A resolution. The enzyme possesses only a single core domain that catalyzes the biological function. No zinc atom is trapped in the active site of the apo structure. Instead, the FucA dimer possesses one sulfate ion per subunit. In chain A the sulfur oxygen atoms are positioned by Asn28, Ser42, Lys46 and Ser68, while in chain B only Asn28, Ser42 and Ser68 take part in the coordination
Q5SHB9
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
-
half-life: 24 h in presence of 0.5 M KH2PO4, half-life: 40 min in presence of 10 mM Tris-HCl
5055
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10-20% of the activity is lost over a period of several months of storage with repeated freezing and thawing
-
15% isopropyl alcohol, enzyme maintains more than 90% of its activity
-
50% acetonitrile, enzyme maintains more than 90% of its activity
-
6 M, urea, enzyme maintains more than 90% of its activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-16C, 10-20% of the activity is lost over a period of several months of storage with repeated freezing and thawing
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation
-
by metal-chelate affinity chromatography and (NH4)2SO4 precipitation after ZnSO4 incubation
-
immobilized metal-chelate affinity column chromatography
-
one step purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M-15 [pREP-4] cells
-
expression in Escherichia coli
-
expression in Escherichia coli XL1 blue MRF cells
-
homologous with the middle domain of L-ribulose-5-phosphate 4-epimerase
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D120N
-
mutant with reduced specific activity
D76E
-
mutant with reduced specific activity
E142Q
-
mutant with increased specific activity
E73Q
-
no enzyme activity
E73Q/Y113F/Y209F
-
no enzyme activity
E73S
-
no enzyme activity
F131A
-
the mutant has 1% retroaldol activity with L-fuculose-1-phosphate as compared to the wild type enzyme. The mutant uses (R)-N-benzyloxycarbonyl-prolinal as substrate and is highly stereoselective both with (R)-and with (S)-N-benzyloxycarbonyl-prolinal, exclusively producing the anti- and syn-aldol adducts, respectively
F131A
-
mutant with improved catalyti activity
F131A/Del(207-215)
-
inactive
F131A/F206A
-
the relative activity of F131A/F206A towards L-fuculose-1-phosphate is approximately less than 0.5% as compared to the wild type enzyme
F131A/Y113A
-
inactive
F206A
-
the mutant has 22% retroaldol activity with L-fuculose-1-phosphate as compared to the wild type enzyme
H218N
-
mutant with reduced specific activity
H97N
-
mutant with reduced specific activity
N28A
-
mutant with reduced specific activity
N29L
-
decreased kcat, increased Km
N29L/S71A
-
no enzyme activity
S71N
-
no enzyme activity
Y113A
-
the mutant has 0.5% retroaldol activity with L-fuculose-1-phosphate as compared to the wild type enzyme
D25L
-
negative effect on catalytic activity and substrate recognition
D25T
-
negative effect on catalytic activity and substrate recognition
K42M
-
mutant with reduced specific activity, can be inhibited by excess Zn2+
additional information
-
the deletion mutants Del(211-215) and Del(207-215) show 11% and 2% retroaldol activity with L-fuculose-1-phosphate, respectively, as compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
a multienzyme system composed by recombinant dihydroxyacetone kinase from Citrobacter freundii, fuculose-1-phosphate aldolase from Escherichia coli and acetate kinase, allows a practical one-pot C-C bond formation catalyzed by dihydroxyacetone phosphate-dependent aldolases from dihydroxyacetone and an aldehyde
synthesis
-
expression of fuculose-1-phosphate aldolase FucA in Escherichia coli as active inclusion bodies in batch cultures and modulation of the activity of insoluble FucA by a proper selection of producing strain, culture media, and process conditions. In an optimized defined medium, FucA inclusion bodies are more active (in terms of specific activity) than the soluble protein version obtained in the same process with a conventional defined medium. Either directly or immobilized into LentikatVR beads, FucA gives product yields ranging from 65 to 76% in an aldolic reaction between DHAP and (S)-Cbz-alaninal