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 hide
4.1.2.17
-
RECOMMENDED NAME
GeneOntology No.
L-fuculose-phosphate aldolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-Fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol addition
-
-
elimination
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)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9024-54-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
r
dihydroxyacetone phosphate + DL-glyceraldehyde
L-tagatose 1-phosphate
show the reaction diagram
dihydroxyacetone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
show the reaction diagram
dihydroxyacetone phosphate + L-lactaldehyde
L-fuculose 1-phosphate
show the reaction diagram
-
-
-
-
r
dihydroxyacetone phosphate + L-lactaldehyde
L-fuculose-1-phosphate
show the reaction diagram
dihydroxyacetone phosphate + L-lactaldehyde
L-rhamnulose-1-phosphate
show the reaction diagram
-
-
-
-
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
-
-
-
r
Glycerone phosphate + (R)-lactaldehyde
6-Deoxy-D-psicose 1-phosphate
show the reaction diagram
Glycerone phosphate + (S)-lactaldehyde
L-Fuculose 1-phosphate
show the reaction diagram
Glycerone phosphate + D-glyceraldehyde
D-Psicose 1-phosphate
show the reaction diagram
glycerone phosphate + DL-glyceraldehyde
?
show the reaction diagram
-
-
-
?
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
show the reaction diagram
Glycerone phosphate + L-glyceraldehyde
L-Tagatose 1-phosphate
show the reaction diagram
L-Fuculose 1-phosphate
?
show the reaction diagram
-
initial step in the metabolism of L-fucose
-
-
-
L-fuculose 1-phosphate
dihydroxyacetone + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
?
L-fuculose 1-phosphate
dihydroxyacetone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
?
L-Fuculose 1-phosphate
Glycerone phosphate + (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
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
?
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
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
additional information
?
-
P0AB87
fucose metabolism
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Mn2+
-
0.01 M, restores activity after dialysis with EDTA; divalent cation required
additional information
no zinc atom is trapped in the active site of the apo structure, crystallization data
INHIBITORS
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.743
D-glyceraldehyde
assay with DL-glyceraldehyde, pH and temperature not specified in the publication
0.091 - 54.7
dihydroxyacetone phosphate
0.743 - 23.1
DL-glyceraldehyde
0.36 - 5
glycerone phosphate
0.5 - 130
L-Fuculose 1-phosphate
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36 - 19.3
dihydroxyacetone phosphate
0.4 - 22
L-Fuculose 1-phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0123
dihydroxyacetone phosphate
direction of aldol condensation, pH not specified in the publication, temperature not specified in the publication
0.01
DL-glyceraldehyde
direction of aldol condensation, pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
in the direction of hydrolysis, pH and temperature not specified in the publication
0.0256
in the direction of aldol condensation, pH and temperature not specified in the publication
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9 - 7.2
-
-
7.5
-
FucA activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
25
-
FucA activity assay
PDB
SCOP
CATH
ORGANISM
UNIPROT
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 hide
LITERATURE
24000
-
monomer
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystallization data
homotetramer
-
-
tetramer
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
-
half-life: 24 h in presence of 0.5 M KH2PO4, half-life: 40 min in presence of 10 mM Tris-HCl
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 hide
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/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
K42M
-
mutant with reduced specific activity, can be inhibited by excess Zn2+
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
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 hide
LITERATURE
synthesis
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