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Information on EC 4.1.2.19 - rhamnulose-1-phosphate aldolase and Organism(s) Escherichia coli and UniProt Accession P32169

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.19 rhamnulose-1-phosphate aldolase
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Escherichia coli
UNIPROT: P32169 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
l-rhamnulose-1-phosphate aldolase, rhamnulose-1-phosphate aldolase, rhamnulose 1-phosphate aldolase, rha-1pa, tm1072, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-Rhamnulose-1-phosphate aldolase
-
L-rhamnulose-1-phosphate aldolase (class II)
-
rhamnulose-1-phosphate aldolase
-
aldolase, rhamnulose phosphate
-
-
-
-
L-Rhamnulose-1-phosphate aldolase
L-Rhamnulose-1-phosphate L-lactaldehyde-lyase
-
-
-
-
Rhamn-1PA
-
-
-
-
rhamnulose 1-phosphate aldolase
-
-
Rhamnulose phosphate aldolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol addition
-
addition
syn-aldol addition
condensation
-
-
-
-
elimination
-
-
aldol addition
-
-
SYSTEMATIC NAME
IUBMB Comments
L-rhamnulose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9054-58-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S,3S)-3-methyl-1-oxopentane-2-benzylcarbamate
(2S,3S,4S,5S)-2-(hydroxymethyl)pyrrolidine-5-((S)-sec-butyl)-3,4-diol + N-ethyl-(2S,3S,4S,5S)-2-(hydroxymethyl)pyrrolidine-5-((S)-sec-butyl)-3,4-diol
show the reaction diagram
-
product ratio 55:45
-
?
(benzyloxy)acetaldehyde + dihydroxyacetone
(3R,4S)-5-(benzyloxy)-1,3,4-trihydroxypentan-2-one + (3R,4R)-5-(benzyloxy)-1,3,4-trihydroxypentan-2-one
show the reaction diagram
favored direction of reaction
-
-
r
(R)-1-oxobutane-2-benzylcarbamate
(2S,3S,4S,5R)-2-(hydroxymethyl)pyrrolidine-5-ethyl-3,4-diol + (2R,3S,4R,5R)-2-(hydroxymethyl)pyrrolidine-5-ethyl-3,4-diol + N-ethyl-(2S,3S,4S,5R)-2-(hydroxymethyl)pyrrolidine-5-ethyl-3,4-diol + N-ethyl-(2R,3S,4R,5R)-2-(hydroxymethyl)pyrrolidine-5-ethyl-3,4-diol
show the reaction diagram
-
product ratio 48:30:11:11
-
?
(R)-1-oxohexane-2-benzylcarbamate
(2S,3S,4S,5R)-2-(hydroxymethyl)pyrrolidine-5-propyl-3,4-diol + (2R,3S,4R,5R)-2-(hydroxymethyl)pyrrolidine-5-propyl-3,4-diol + N-ethyl-(2R,3S,4R,5R)-2-(hydroxymethyl)pyrrolidine-5-propyl-3,4-diol + N-ethyl-(2S,3S,4S,5R)-2-(hydroxymethyl)-pyrrolidine-5-propyl-3,4-diol
show the reaction diagram
-
product ratio 28:63:5:5
-
?
(R)-1-oxopentane-2-benzylcarbamate
(2S,3S,4S,5R)-2-(hydroxymethyl)pyrrolidine-5-propyl-3,4-diol + (2R,3S,4R,5R)-2-(hydroxymethyl)pyrrolidine-5-propyl-3,4-diol + N-ethyl-(2S,3S,4S,5R)-2-(hydroxymethyl)pyrrolidine-5-propyl-3,4-diol + N-ethyl-(2R,3S,4R,5R)-2-(hydroxymethyl)pyrrolidine-5-propyl-3,4-diol
show the reaction diagram
-
product ratio 44:34:11:10
-
?
(R)-3-methyl-1-oxobutane-2-benzylcarbamate
(2R,3S,4R,5R)-2-(hydroxymethyl)pyrrolidine-5-isopropyl-3,4-diol
show the reaction diagram
-
-
-
?
(R)-4-methyl-1-oxopentane-2-benzylcarbamate
(2S,3S,4S,5R)-2-(hydroxymethyl)pyrrolidine-5-isobutyl-3,4-diol + (2R,3S,4R,5R)-2-(hydroxymethyl)pyrrolidine-5-isobutyl-3,4-diol + N-ethyl-(2R,3S,4R,5R)-2-(hydroxymethyl)pyrrolidine-5-isobutyl-3,4-diol + N-ethyl-(2S,3S,4S,5R)-2-(hydroxymethyl)pyrrolidine-5-isobutyl-3,4-diol
show the reaction diagram
-
product ratio 32:43:16.9
-
?
(S)-1-oxo-3-phenylpropan-2-benzylcarbamate
(2S,3S,4S,5S)-2-(hydroxymethyl)pyrrolidine-5-benzyl-3,4-diol
show the reaction diagram
-
-
-
?
(S)-1-oxobutane-2-benzylcarbamate
(2S,3S,4S,5S)-2-(hydroxymethyl)pyrrolidine-5-ethyl-3,4-diol
show the reaction diagram
-
-
-
?
(S)-1-oxohexane-2-benzylcarbamate
(2S,3S,4S,5S)-2-(hydroxymethyl)pyrrolidine-5-butyl-3,4-diol + (2S,3S,4R,5S)-2-(hydroxymethyl)pyrrolidine-5-butyl-3,4-diol
show the reaction diagram
-
product ratio 93:7
-
?
(S)-1-oxopentane-2-benzylcarbamate
(2S,3S,4S,5S)-2-(hydroxymethyl)pyrrolidine-5-propyl-3,4-diol
show the reaction diagram
-
-
-
?
(S)-3-methyl-1-oxobutane-2-benzylcarbamate
(2S,3S,4S,5S)-2-(hydroxymethyl)pyrrolidine-5-isopropyl-3,4-diol + N-ethyl-(2S,3S,4S,5S)-2-(hydroxymethyl)pyrrolidine-5-isopropyl-3,4-diol
show the reaction diagram
-
product ratio 84:16
-
?
(S)-4-methyl-1-oxopentane-2-benzylcarbamate
(2S,3S,4S,5S)-2-(hydroxymethyl)pyrrolidine-5-isobutyl-3,4-diol + (2S,3S,4R,5S)-2-(hydroxymethyl)pyrrolidine-5-isobutyl-3,4-diol + N-ethyl-(2S,3S,4S,5S)-2-(hydroxymethyl)pyrrolidine-5-isobutyl-3,4-diol
show the reaction diagram
-
product ratio 71:6:23
-
?
2-methyl-1-oxopropane-2-benzylcarbamate
(2S,3S,4S)-2-(hydroxymethyl)pyrrolidine-5-dimethyl-3,4-diol + (2R,3S,4R)-2-(hydroxymethyl)pyrrolidine-5-dimethyl-3,4-diol
show the reaction diagram
-
product ratio 44:56
-
?
benzyl (2-oxoethyl)carbamate + dihydroxyacetone
benzyl [(2S,3R)-2,3,5-trihydroxy-4-oxopentyl]carbamate + benzyl [(2R,3R)-2,3,5-trihydroxy-4-oxopentyl]carbamate
show the reaction diagram
favored direction of reaction
-
-
r
benzyl [(2R)-1-oxopropan-2-yl]carbamate + dihydroxyacetone
benzyl [(2R,3S,4R)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate + benzyl [(2R,3R,4R)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate
show the reaction diagram
favored direction of reaction
-
-
r
dihydroxyacetone + L-lactaldehyde
L-rhamnulose 1-phosphate
show the reaction diagram
favored direction of reaction
-
-
r
dihydroxyacetone phosphate + L-lactaldehyde
?
show the reaction diagram
-
-
-
?
dihydroxyacetone phosphate + L-lactaldehyde
L-rhamnulose 1-phosphate
show the reaction diagram
glycerone phosphate + D-glyceraldehyde
D-psicose 1-phosphate
show the reaction diagram
-
-
-
?
glycerone phosphate + D-glyceraldehyde
D-sorbose 1-phosphate
show the reaction diagram
-
-
-
?
glycerone phosphate + L-glyceraldehyde
L-fructose 1-phosphate
show the reaction diagram
-
-
-
?
glycerone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
show the reaction diagram
-
-
-
?
L-rhamnulose 1-phosphate
dihydroxyacetone phosphate + L-lactaldehyde
show the reaction diagram
-
-
-
r
L-Rhamnulose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
N-formylglycinal + dihydroxyacetone
N-[(2S,3R)-2,3,5-trihydroxy-4-oxopentyl]formamide + N-[(2R,3R)-2,3,5-trihydroxy-4-oxopentyl]formamide
show the reaction diagram
-
-
-
r
(2R)-2,3-dihydroxy-4-nitrobutanal
(1R,2R,3S,4R,5S,6S)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3,4,5-pentol + (1S,2R,3R,4R,5R,6R)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3,4,5-pentol
show the reaction diagram
-
-
-
-
r
(2S)-2,3-dihydroxy-4-nitrobutanal
(1R,2R,3S,4S,5S,6S)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3,4,5-pentol + 1-hydroxymethyl-6-nitrocyclohexane-1,2,3,4,5-pentol
show the reaction diagram
-
-
-
-
r
3-hydroxy-4-nitrobutanal
(1R,2R,3S,5R,6S)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3,5-tetraol + (1S,2R,3R,5S,6R)-1-hydroxymethyl-6-nitrocyclohexane-1,2,3,5-tetraol
show the reaction diagram
-
-
-
-
r
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
show the reaction diagram
-
-
-
-
?
6-Deoxy-L-sorbose 1-phosphate
Glycerone phosphate + D-lactaldehyde
show the reaction diagram
-
0.8% of the activity with L-rhamnulose 1-phosphate
-
-
?
D-Fructose 1-phosphate
?
show the reaction diagram
-
1.7% of the activity with L-rhanmnulose 1-phosphate
-
-
?
D-Fructose-1,6-diphosphate
?
show the reaction diagram
-
1.8% of the activity with L-rhanmnulose 1-phosphate
-
-
?
D-Ribulose 1,5-diphosphate
?
show the reaction diagram
-
1.3% of the activity with L-rhanmnulose 1-phosphate
-
-
?
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
-
-
yield 93%, ratio of (3R,4S) to (3S,4R) product is 2:98
-
?
dihydroxyacetone phosphate + N-Cbz-(2S)-2-amino-3-methylbutanal
N-Cbz-5-amino-1,3,4-trihydroxyoctan-2-one
show the reaction diagram
-
-
yield 93%, ratio of (3R,4S) to (3S,4R) product is 98:2
-
?
dihydroxyacetone phosphate + N-Cbz-(2S)-2-aminobutanal
N-Cbz-5-amino-1,3,4-trihydroxyheptan-2-one
show the reaction diagram
-
-
yield 94%, ratio of (3R,4S) to (3S,4R) product is 98:2
-
?
dihydroxyacetone phosphate + N-Cbz-(2S)-2-aminopropanal
N-Cbz-5-amino-1,3,4-trihydroxyhexan-2-one
show the reaction diagram
-
-
yield 99%, ratio of (3R,4S) to (3S,4R) product is 98:2
-
?
dihydroxyacetone phosphate + N-Cbz-aminoacetaldehyde
N-Cbz-5-amino-1,3,4-trihydroxypentan-2-one
show the reaction diagram
-
yield 91%, ratio of (3R,4S) to (3S,4R) product is 94:6
yield 91%, ratio of (3R,4S) to (3S,4R) product is 94:6
-
?
dimethoxyacetaldehyde + glycerone phosphate
(3R,4R)-3,4-dihydroxy-5,5-dimethoxy-2-oxopentyl phosphate
show the reaction diagram
-
-
-
-
?
Glycerone phosphate + (S)-lactaldehyde
L-Rhamnulose 1-phosphate
show the reaction diagram
Glycerone phosphate + acetaldehyde
5-Deoxy-L-xylulose 1-phosphate
show the reaction diagram
glycerone phosphate + D-glyceraldehyde
D-sorbose 1-phosphate
show the reaction diagram
Glycerone phosphate + D-lactaldehyde
6-Deoxy-D-sorbose 1-phosphate
show the reaction diagram
Glycerone phosphate + formaldehyde
D-Erythrulose 1-phosphate
show the reaction diagram
Glycerone phosphate + glycolaldehyde
L-Xylulose 1-phosphate
show the reaction diagram
L-Rhamnulose 1-phosphate
?
show the reaction diagram
-
-
-
-
?
L-rhamnulose 1-phosphate
dihydroxyacetone phosphate + L-lactaldehyde
show the reaction diagram
-
-
-
-
r
L-Rhamnulose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
L-Sorbose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
Xylulose 1-phosphate
Glycerone phosphate + glycoaldehyde
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Rhamnulose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
-
-
-
?
L-Rhamnulose 1-phosphate
?
show the reaction diagram
-
-
-
-
?
L-rhamnulose 1-phosphate
dihydroxyacetone phosphate + L-lactaldehyde
show the reaction diagram
-
-
-
-
r
L-Rhamnulose 1-phosphate
Glycerone phosphate + (S)-lactaldehyde
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
restores activity of the enzyme after inactivation by dialysis against chelating agents or by treatment with SDS and 2-mercaptoethanol
Cs+
-
Na+, Cs+, NH4+, Rb+ and K+, in the order of increasing effectiveness markedly enhance activity
K+
-
Na+, Cs+, NH4+, Rb+ and K+, in the order of increasing effectiveness markedly enhance activity
Na+
-
Na+, Cs+, NH4+, Rb+ and K+, in the order of increasing effectiveness markedly enhance activity
NH4+
-
Na+, Cs+, NH4+, Rb+ and K+, in the order of increasing effectiveness markedly enhance activity
Ni2+
-
restores activity of the enzyme after inactivation by dialysis against chelating agents or by treatment with SDS and 2-mercaptoethanol
Rb+
-
Na+, Cs+, NH4+, Rb+ and K+, in the order of increasing effectiveness markedly enhance activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
the aldol addition of dihydroxyacetobe is strongly inhibited by phosphate
1,10-phenanthroline
2,2'-dipyridyl
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
8-hydroxyquinoline 5-sulfonic acid
-
-
HgCl2
-
reversible
L-Rhamnitol 1-phosphate
-
-
p-mercuribenzoate
SDS
-
competitive with L-rhamnulose 1-phosphate or glycerone phosphate, noncompetitive with L-lactaldehyde
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the enzyme contains 12 sulfhydryl groups per molecule
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1125 - 1339
dihydroxyacetone
0.6 - 7
dihydroxyacetone phosphate
1.9 - 5.4
L-rhamnulose 1-phosphate
1.8
D-sorbose 1-phosphate
-
-
0.2 - 3
glycerone phosphate
0.1 - 6
L-lactaldehyde
0.2 - 10
L-rhamnulose 1-phosphate
0.2
L-xylulose 1-phosphate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.1
dihydroxyacetone phosphate
-
38.3
L-rhamnulose 1-phosphate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
Co2+
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
phosphate
Escherichia coli
wild type enzyme, at pH 7.0 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
mutant enzyme S75D, using L-rhamnulose-1-phosphate as substrate, at pH 7.0 and 25°C
0.005
mutant enzyme N32D, using L-rhamnulose-1-phosphate as substrate, at pH 7.0 and 25°C
0.006
mutant enzyme S116D, using L-rhamnulose-1-phosphate as substrate, at pH 7.0 and 25°C
0.2
mutant enzyme N29D, using L-rhamnulose-1-phosphate as substrate, at pH 7.0 and 25°C
3.8
wild type enzyme, using L-rhamnulose-1-phosphate as substrate, at pH 7.0 and 25°C
3.3
-
enzyme activity in culture performed at 37°C
4.2
-
enzyme activity in culture performed at 28°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH 6.0: about 30% of maximal activity, pH 9.9: about 50% of maximal activity
6.3 - 9
-
about 50% of maximal activity at pH 6.3 and at pH 9.0
8.5 - 9.9
-
pH 8.5: about 50% of maximal activity, pH 9.9: about 70% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000 - 140000
-
sucrose density gradient centrifugation
135000
-
gel filtration
140000
-
gel filtration, density gradient centrifugation
32000
-
determined by SDS-PAGE
35000
-
4 * 35000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
-
tetramer
-
4 * 35000
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, crystallizes in space group P3(2)21
mutant enzymes by hanging drop vapour diffusion method, with 100 mM sodium acetate pH 4.5, 50% (v/v) ethylene glycol and 5% (w/v) PEG1000
structure established at 1.35 A resolution in a crystal form that is obtained by a surface mutation and has one subunit of the C4-symmetric tetramer in the asymmetric unit. Crystals of the wild-type enzyme with their 20 crystallographically asymmetric subunits diffract to only 2.7 A resolution are much too complex for a convenient analysis of structural modifications. For both reasons, a more suitable crystal form is obtained by producing the six point mutants W8T, Q51R, Q52E, D98Y, E192A and E254R at the protein surface far away from the active center
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E117Q
0.1% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 0.04% of the wild-type ratio
E171A
0.4% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 0.3% of the wild-type ratio
E171Q
0.4% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 0.1% of the wild-type ratio
E171S
2% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 0.7% of the wild-type ratio
E192A
as active as the wild-type enzyme with L-rhamnulose 1-phosphate
G264Stop
75% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as 23% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 7% of the wild-type ratio
K15W
reduced activity
K15Y
reduced activity
K248G/R253A/E254A/E192A
reduced activity
L84W
reduced activity
N29A
4% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 0.9% of the wild-type ratio
N29D
the mutant shows 5.3% of the wild type activity, the mutation increases by 3fold the Vappmax of aldol addition reactions of dihydroxyacetone to other aldehyde acceptors rather than the natural L-lactaldehyde
N32D
the mutant shows 0.1% of the wild type activity
Q11W
reduced activity
R28S
9% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 2% of the wild-type ratio
S116D
the mutant shows 0.2% of the wild type activity
S75D
the mutant shows 0.1% of the wild type activity
T115D
completely inactive
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
0-4°C, stable for at least 3 months
5049
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sulfhydryl compounds stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C, crystalline enzyme, containing 0.2-1.0% protein, stable for at least 3 months
-
0-4°C, pH 7.0, 0.01 M mercaptoethanol, stable for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HR 16/40 afinity column chromatography
Superdex 200 gel filtration
Ni-NTA column chromatography
-
only 55% of immobilization yield is achieved when immobilized metal affinity chromatography is used to purify and immobilize RhuA from cellular lysate in a single step
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain JM105
expressed in Escherichia coli strain M-15
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli strain BL21 (DE3)
-
expression in Escherichia coli cells
-
His-tagged enzyme is expressed in Escherichia coli M15DELTAglyA cells
-
overexpression in Escherichia coli
-
overexpression in Escherichia coli cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Feingold, D.S.; Hoffee, P.A.
Other deoxy sugar aldolases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
303-321
1972
Escherichia coli, Lactiplantibacillus plantarum
-
Manually annotated by BRENDA team
Garcia-Junceda, E.; Shen, G.J.; Sugai, T.; Wong, C.H.
A new strategy for the cloning, overexpression and one step purification of three DHAP-dependent aldolases: rhamnulose-1-phosphate aldolase, fuculose-1-phosphate aldolase and tagatose-1,6-diphosphate aldolase
Bioorg. Med. Chem.
3
945-953
1995
Escherichia coli
Manually annotated by BRENDA team
Sawada, H.; Takagi, Y.
The metabolism of L-rhamnose in Escherichia coli
Biochim. Biophys. Acta
92
26-32
1964
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Chiu, T.H.; Feingold, D.S.
L-Rhamnulose 1-phosphate aldolase from Escherichia coli. Crystallization and properties
Biochemistry
8
98-108
1969
Escherichia coli
Manually annotated by BRENDA team
Takagi, Y.
L-Rhamnulose 1-phosphate aldolase
Methods Enzymol.
9
542-545
1966
Escherichia coli, Escherichia coli B / ATCC 11303
-
Manually annotated by BRENDA team
Schwartz, N.B.; Feingold, D.S.
L-Rhamnulose 1-phosphate aldolase from Escherichia coli. III. The role of divalent cations in enzyme activity
Bioorg. Chem.
2
75-86
1972
Escherichia coli
-
Manually annotated by BRENDA team
Schwartz, N.B.; Abram, D.; Feingold, D.S.
L-Rhamnulose 1-phosphate aldolase of Escherichia coli. The role of metal in enzyme structure
Biochemistry
13
1726-1730
1974
Escherichia coli
Manually annotated by BRENDA team
Chiu, T.H.; Evans, K.L.; Feingold, D.S.
L-Rhamnulose-1-phosphate aldolase
Methods Enzymol.
42C
264-269
1975
Escherichia coli, Escherichia coli K40
-
Manually annotated by BRENDA team
Kroemer, M.; Schulz, G.E.
The structure of L-rhamnulose-1-phosphate aldolase (class II) solved by low-resolution SIR phasing and 20-fold NCS averaging
Acta Crystallogr. Sect. D
58
824-832
2002
Escherichia coli (P32169)
Manually annotated by BRENDA team
Kroemer, M.; Merkel, I.; Schulz, G.E.
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase
Biochemistry
42
10560-10568
2003
Escherichia coli (P32169)
Manually annotated by BRENDA team
Franke, D.; Machajewski, T.; Hsu, C.C.; Wong, C.H.
One-pot synthesis of L-fructose using coupled multienzyme systems based on rhamnulose-1-phosphate aldolase
J. Org. Chem.
68
6828-6831
2003
Escherichia coli
Manually annotated by BRENDA team
Grueninger, D.; Schulz, G.E.
Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase
Biochemistry
47
607-614
2008
Escherichia coli (P32169), Escherichia coli
Manually annotated by BRENDA team
Sugiyama, M.; Hong, Z.; Greenberg, W.A.; Wong, C.H.
In vivo selection for the directed evolution of L-rhamnulose aldolase from L-rhamnulose-1-phosphate aldolase (RhaD)
Bioorg. Med. Chem.
15
5905-5911
2007
Escherichia coli, Escherichia coli W3110 / ATCC 27325
Manually annotated by BRENDA team
Jimenez, A.; Clapes, P.; Crehuet, R.
Protein flexibility and metal coordination changes in DHAP-dependent aldolases
Chemistry
15
1422-1428
2009
Escherichia coli (P32169)
Manually annotated by BRENDA team
Pinsach, J.; de Mas, C.; Lopez-Santin, J.; Striedner, G.; Bayer, K.
Influence of process temperature on recombinant enzyme activity in Escherichia coli fed-batch cultures
Enzyme Microb. Technol.
43
507-512
2008
Escherichia coli
-
Manually annotated by BRENDA team
Vidal, L.; Pinsach, J.; Striedner, G.; Caminal, G.; Ferrer, P.
Development of an antibiotic-free plasmid selection system based on glycine auxotrophy for recombinant protein overproduction in Escherichia coli
J. Biotechnol.
134
127-136
2008
Escherichia coli
Manually annotated by BRENDA team
Calveras, J.; Egido-Gabas, M.; Gomez, L.; Casas, J.; Parella, T.; Joglar, J.; Bujons, J.; Clapes, P.
Dihydroxyacetone phosphate aldolase catalyzed synthesis of structurally diverse polyhydroxylated pyrrolidine derivatives and evaluation of their glycosidase inhibitory properties
Chemistry
15
7310-7328
2009
Escherichia coli (P32169), Escherichia coli
Manually annotated by BRENDA team
Ruiz, J.; Pinsach, J.; Alvaro, G.; Gonzlez, G.; de Mas, C.; Resina, D.; Lopez-Santin, J.
Alternative production process strategies in E. coli improving protein quality and downstream yields
Process Biochem.
44
1039-1045
2009
Escherichia coli
-
Manually annotated by BRENDA team
Garrabou, X.; Joglar, J.; Parella, T.; Crehuet, R.; Bujons, J.; Claps, P.
Redesign of the phosphate binding site of L-rhamnulose-1-phosphate aldolase towards a dihydroxyacetone dependent aldolase
Adv. Synth. Catal.
353
89-99
2011
Escherichia coli (P32169)
-
Manually annotated by BRENDA team
Ardao, I.; Comenge, J.; Benaiges, M.D.; Alvaro, G.; Puntes, V.F.
Rational nanoconjugation improves biocatalytic performance of enzymes: aldol addition catalyzed by immobilized rhamnulose-1-phosphate aldolase
Langmuir
28
6461-6467
2012
Escherichia coli
Manually annotated by BRENDA team
Garrabou, X.; Calveras, J.; Joglar, J.; Parella, T.; Bujons, J.; Clapes, P.
Highly efficient aldol additions of DHA and DHAP to N-Cbz-amino aldehydes catalyzed by L-rhamnulose-1-phosphate and L-fuculose-1-phosphate aldolases in aqueous borate buffer
Org. Biomol. Chem.
9
8430-8436
2011
Escherichia coli
Manually annotated by BRENDA team
Camps Bres, F.; Guerard-Hlaine, C.; Hlaine, V.; Fernandes, C.; Sanchez-Moreno, I.; Traikia, M.; Garcia-Junceda, E.; Lemaire, M.
L-Rhamnulose-1-phosphate and L-fuculose-1-phosphate aldolase mediated multi-enzyme cascade systems for nitrocyclitol synthesis
J. Mol. Catal. B
114
50-57
2015
Escherichia coli
-
Manually annotated by BRENDA team
Lee, S.H.; Hong, S.H.; An, J.U.; Kim, K.R.; Kim, D.E.; Kang, L.W.; Oh, D.K.
Structure-based prediction and identification of 4-epimerization activity of phosphate sugars in class II aldolases
Sci. Rep.
7
1934
2017
Escherichia coli (P32169)
Manually annotated by BRENDA team