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 ACCESSION NO.
LITERATURE
L-Fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
-
L-Fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldol addition
-
-
elimination
-
-
elimination
-
-
of an aldehyde, C-C bond cleavage
-
PATHWAY
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
-
fucose degradation
-
lactate biosynthesis (archaea)
-
SYSTEMATIC NAME
IUBMB Comments
L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldolase, L-fuculose phosphate
-
-
-
-
Fuc-1PA
-
-
-
-
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-1-phosphate aldolase
-
-
L-fuculose-1-phosphate aldolase
-
-
L-fuculose-phosphate aldolase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-54-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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 ACCESSION NO.
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 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
DL-glycerol 3-phosphate + D-glyceraldehyde
?
show the reaction diagram
-
-
-
-
?
DL-glycerol 3-phosphate + dihydroxyacetone phosphate
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
additional information
?
-
P0AB87
fucose metabolism
-
?
additional information
?
-
-
(R)-N-benzyloxycarbonyl-prolinal is not a substrate for the wild type enzyme
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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
Mn2+
-
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
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
-
diethyldicarbonate
-
inactivates at 5 mM, rate is dependent on pH, glycerone phosphate protects
L-fagomine
-
-
-
Methylglyoxal
-
competitive inhibition
Phosphoglycolohydroxamate
-
-
Zn2+
-
inhibitory effect of Zn2+ on his-tagged enzyme, but not on the native enzyme
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
54.7
-
dihydroxyacetone phosphate
-
-
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
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.9
7.2
-
-
7.5
-
-
FucA activity assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
FucA activity assay
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24000
-
-
monomer
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
homotetramer
-
-
tetramer
-
4 * 23775, calculation from nucleotide sequence
tetramer
-
4 * 24000
tetramer
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
LITERATURE
expressed in Escherichia coli M-15 [pREP-4] cells
-
expression in Escherichia coli XL1 blue MRF cells
-
homologous with the middle domain of L-ribulose-5-phosphate 4-epimerase
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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/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 ACCESSION NO.
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