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Information on EC 4.1.2.17 - L-fuculose-phosphate aldolase and Organism(s) Escherichia coli and UniProt Accession P0AB87
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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 taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldolase, L-fuculose phosphate
-
-
-
-
Fuc-1PA
-
-
-
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L-Fuculose 1-phosphate aldolase
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-
-
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L-Fuculose phosphate aldolase
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-
-
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L-Fuculose-1-P aldolase
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-
-
-
L-fuculose-1-phosphate aldolase
L-fuculose-1-phosphate aldolase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9024-54-8
-
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
-
-
-
?
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
-
-
-
?
dimethoxyacetaldehyde + glycerone phosphate
(3R,4S)-3,4-dihydroxy-5,5-dimethoxy-2-oxopentyl phosphate
-
-
-
?
Glycerone phosphate + (S)-lactaldehyde
L-Fuculose 1-phosphate
-
-
-
?
glycerone phosphate + L-glyceraldehyde
L-fructose 1-phosphate
-
-
-
?
glycerone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
-
-
-
?
(S)-Cbz-alaninal + dihydroxyacetone phosphate
(3R,4R,5S)-5-(benzyloxycarbonylamino)-5,6-dideoxy-1-phosphonohex-2-ulose
-
-
-
-
?
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
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-
-
-
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
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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
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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
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wild-type 63% aldol adduct formed, mutant F131A, 50% aldol adduct formed
-
-
?
L-fuculose 1-phosphate
dihydroxyacetone phosphate + (S)-lactaldehyde
-
-
-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
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-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
r
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
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at 73% of the activity with (S)-lactaldehyde
-
?
glycerone phosphate + D-glyceraldehyde
D-psicose 1-phosphate
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at 33% of the activity with (S)-lactaldehyde
-
-
?
glycerone phosphate + D-glyceraldehyde
D-psicose 1-phosphate
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at 33% of the activity with (S)-lactaldehyde
-
?
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
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at 10% of the activity with (S)-lactaldehyde
-
-
?
Glycerone phosphate + glycolaldehyde
D-Ribulose 1-phosphate
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at 10% of the activity with (S)-lactaldehyde
-
?
glycerone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
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at 33% of the activity with (S)-lactaldehyde
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-
?
glycerone phosphate + L-glyceraldehyde
L-tagatose 1-phosphate
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at 33% of the activity with (S)-lactaldehyde
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
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-
-
r
additional information
?
-
-
(R)-N-benzyloxycarbonyl-prolinal is not a substrate for the wild type enzyme
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-
?
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
Glycerone phosphate + (S)-lactaldehyde
L-Fuculose 1-phosphate
-
-
-
?
dihydroxyacetone phosphate + L-lactaldehyde
L-fuculose 1-phosphate
-
-
-
-
r
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
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-
-
?
L-fuculose 1-phosphate
glycerone phosphate + (S)-lactaldehyde
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
-
can substitute for the naturally occuring Zn2+, with somewhat higher activity
Mg2+
Mn2+
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Zn2+
-
inhibitory effect of Zn2+ on his-tagged enzyme, but not on the native enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
19
L-Fuculose 1-phosphate
pH 7.5, 37°C, wild-type enzyme and E214A mutant
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4 - 8.8
-
pH 6.4: about 30% of maximal activity, pH 8.8: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F131A
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
F206A
-
the mutant has 22% retroaldol activity with L-fuculose-1-phosphate as compared to the wild type enzyme
K42M
-
mutant with reduced specific activity, can be inhibited by excess Zn2+
Y113A
-
the mutant has 0.5% retroaldol activity with L-fuculose-1-phosphate as compared to the wild type enzyme
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
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
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-16°C, 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
by metal-chelate affinity chromatography and (NH4)2SO4 precipitation after ZnSO4 incubation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, Y.M.; Zhu, Y.; Lin, E.C.C.
The organization of the fuc regulon specifying L-fucose dissimilation in Escherichia coli K12 as determined by gene cloning
Mol. Gen. Genet.
210
331-337
1987
Escherichia coli
Ghalambor, M.A.; Heath, E.C.
The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate
J. Biol. Chem.
237
2427-2433
1962
Escherichia coli
Ghalambor, M.A.; Heath, E.C.
L-Fuculose 1-phosphate aldolase
Methods Enzymol.
9
538-542
1966
Escherichia coli, Escherichia coli 0111-B4
-
Feingold, D.S.; Hoffee, P.A.
Other deoxy sugar aldolases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
303-321
1972
Escherichia coli, Escherichia coli 0111-B4
-
Hixon, M.; Sinerius, G.; Schneider, A.; Walter, C.; Fessner, W.D.; Schloss, J.V.
Quo vadis photorespiration: a tale of two aldolases
FEBS Lett.
392
281-284
1996
Escherichia coli
Dreyer, M.K.; Schulz, G.E.
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure
J. Mol. Biol.
259
458-466
1996
Escherichia coli
Dreyer, M.K.; Schulz, G.E.
The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli
J. Mol. Biol.
231
549-553
1993
Escherichia coli
Dreyer, M.K.; Schulz, G.E.
Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli
Acta Crystallogr. Sect. D
52
1082-1091
1996
Escherichia coli
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
Joerger, A.C.; Gosse, C.; Fessner, W.D.; Schulz, G.E.
Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis
Biochemistry
39
6033-6041
2000
Escherichia coli (P0AB87)
Samuel, J.; Luo, Y.; Morgan, P.M.; Strynadka, N.C.; Tanner, M.E.
Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison with L-fuculose-1-phosphate aldolase
Biochemistry
40
14772-14780
2001
Escherichia coli
Joerger, A.C.; Mueller-Dieckmann, C.; Schulz, G.E.
Structures of L-fuculose-1-phosphate aldolase mutants outlining motions during catalysis
J. Mol. Biol.
303
531-543
2000
Escherichia coli (P0AB87)
Sanchez-Moreno, I.; Garcia-Garcia, J.F.; Bastida, A.; Garcia-Junceda, E.
Multienzyme system for dihydroxyacetone phosphate-dependent aldolase catalyzed C-C-bond formation from dihydroxyacetone
Chem. Commun. (Camb.)
2004
1634-1635
2004
Escherichia coli
-
Ardao, I.; Benaiges, M.D.; Caminal, G.; Alvaro, G.
One step purification-immobilization of fuculose-1-phosphate aldolase, a class II DHAP dependent aldolase, by using metal-chelate supports
Enzyme Microb. Technol.
39
22-27
2006
Escherichia coli
-
Suau, T.; Alvaro, G.; Benaiges, M.D.; Lopez-Santin, J.
Kinetic modelling of aldolase-catalyzed addition between dihydroxyacetone phosphate and (S)-alaninal
Biochem. Eng. J.
41
95-103
2008
Escherichia coli
-
Jimenez, A.; Clapes, P.; Crehuet, R.
Protein flexibility and metal coordination changes in DHAP-dependent aldolases
Chemistry
15
1422-1428
2009
Escherichia coli
Garrabou, X.; Gomez, L.; Joglar, J.; Gil, S.; Parella, T.; Bujons, J.; Clapes, P.
Structure-guided minimalist redesign of the L-fuculose-1-phosphate aldolase active site: expedient synthesis of novel polyhydroxylated pyrrolizidines and their inhibitory properties against glycosidases and intestinal disaccharidases
Chemistry
16
10691-10706
2010
Escherichia coli
Sans, C.; Garcia-Fruitos, E.; Ferraz, R.M.; Gonzalez-Montalban, N.; Rinas, U.; Lopez-Santin, J.; Villaverde, A.; Alvaro, G.
Inclusion bodies of fuculose-1-phosphate aldolase as stable and reusable biocatalysts
Biotechnol. Prog.
28
421-427
2012
Escherichia coli
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
Li, A.; Cai, L.; Chen, Z.; Wang, M.; Wang, N.; Nakanishi, H.; Gao, X.D.; Li, Z.
Recent advances in the synthesis of rare sugars using DHAP-dependent aldolases
Carbohydr. Res.
452
108-115
2017
Escherichia coli (P0AB87)
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 (P0AB87)
-
Li, Z.J.; Hong, P.H.; Da, Y.Y.; Li, L.K.; Stephanopoulos, G.
Metabolic engineering of Escherichia coli for the production of L-malate from xylose
Metab. Eng.
48
25-32
2018
Escherichia coli
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