Information on EC 4.2.1.68 - L-fuconate dehydratase

Substrates: -
Products: -

D-gluconate

Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7

Substrates: -
Products: -

L-fuconate

2-dehydro-3-deoxy-L-fuconate + H2O

Substrates: -
Products: -

L-fuconate

2-dehydro-3-deoxy-L-fuconate + H2O

Substrates: -
Products: -

L-fuconate

2-dehydro-3-deoxy-L-fuconate + H2O

33952

Substrates: -
Products: -

L-fuconate

2-dehydro-3-deoxy-L-fuconate + H2O

Substrates: FucD reaction involves initial abstraction of the 2-proton by Lys220, acid catalysis of the vinylogous beta-elimination of the 3-OH group by His351, and stereospecific ketonization of the resulting enol, likely by the conjugate acid of Lys220, to yield the 2-keto-3-deoxy-L-fuconate product
Products: -

L-Fuconate

Substrates: -
Products: -

L-Fuconate

Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7

Substrates: -
Products: -

L-Fuconate

Substrates: catabolism of L-fucose
Products: -

L-Fuconate

33951, 33952

Substrates: catabolism of L-fucose
Products: -

L-fuconate + H2O

2-dehydro-3-deoxy-L-fuconate

Substrates: highly preferred enzyme
Products: -

L-fuconate + H2O

2-dehydro-3-deoxy-L-fuconate

Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7

Substrates: highly preferred enzyme
Products: -

L-galactonate

2-dehydro-3-deoxy-L-galactonate + H2O

Substrates: -
Products: -

L-galactonate

2-dehydro-3-deoxy-L-galactonate + H2O

Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7

Substrates: -
Products: -

L-galactonate

2-keto-3-deoxy-L-galactonate + H2O

Substrates: -
Products: -

L-galactonate

2-keto-3-deoxy-L-galactonate + H2O

33952

Substrates: -
Products: -

L-galactonate

2-keto-3-deoxy-L-galactonate + H2O

Substrates: dehydration of L-galactonate is initiated by abstraction of the 2-proton by Lys220
Products: -

L-mannonate

2-dehydro-3-deoxy-L-mannonate + H2O

Substrates: -
Products: -

L-mannonate

2-dehydro-3-deoxy-L-mannonate + H2O

Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7

Substrates: -
Products: -

show all columns Go to Natural Substrate Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

L-Fuconate

2 entries

L-Fuconate

Substrates: catabolism of L-fucose
Products: -

L-Fuconate

33951, 33952

Substrates: catabolism of L-fucose
Products: -

show all columns Go to Metals and Ions Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Mg2+

required for activity

show all columns Go to Inhibitor Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

D-arabonate

10 mM, 100% inhibition

D-arabono-1,5-lactone

D-galactonate

10 mM, 100% inhibition

D-gluconate

10 mM, 100% inhibition

EDTA

10 mM, 100% inhibition

HgCl2

0.25 mM, ca. 90% inhibition

iodoacetate

2.5 mM, 90% inhibition

L-Rhamnonate

10 mM, 95% inhibition

N-ethylmaleimide

1 mM, 81% inhibition

p-chloromercuribenzoate

0.25 mM, 79% inhibition

p-hydroxymercuribenzoate

ZnSO4

5 mM, 78% inhibition

show all columns Go to KM Value Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2.1

D-Arabinonate

25°C, pH 7.5

1.3

L-arabonate

0.33 - 1.89

L-fuconate

4 entries

3.3 - 6.2

L-galactonate

3 entries

additional information

Michaelis-Menten kinetics

0.33

L-fuconate

25°C, pH 7.5

0.6

L-fuconate

L-fuconate

1.89

L-fuconate

recombinant enzyme, pH 7.0, temperature not specified in the publication

3.3

L-galactonate

3.92

L-galactonate

recombinant enzyme, pH 7.0, temperature not specified in the publication

6.2

L-galactonate

25°C, pH 7.5

show all columns Go to Turnover Number Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2.4

D-Arabinonate

25°C, pH 7.5

L-fuconate

25°C, pH 7.5

0.9

L-galactonate

25°C, pH 7.5

show all columns Go to Specific Activity Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.066

29.1

show all columns Go to pH Optimum Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

6.8 - 7.4

show all columns Go to pH Range Search

assay at

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 - 9

less than 50% of maximal activity above and below

show all columns Go to Temperature Optimum Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

show all columns Go to Temperature Range Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

30 - 50

less than 50% of maximal activity above and below

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

UniProt

brenda

Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7

UniProt

brenda

brenda

33951, 33952

brenda

pv. campestris str. ATCC 33913

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

brenda

brenda

poor source

brenda

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Show AA Sequence and Transmembrane Helices (3749 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.

Go to PDB and Structure Links Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

PDB

SCOP

CATH

UNIPROT

ORGANISM

Xanthomonas campestris pv. campestris

show all columns Go to Molecular Weight Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

104000

sucrose density ultracentifugation

95000

gel filtration

Go to General Stability Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

very unstable, not stabilized by MgCl2 or EDTA

Go to Storage Stability Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-20°C, 30% loss of activity in 1 month

-60°C, 5 mM dithiothreitol, 2mg/ml protein, stable for 1 month

Go to Purification (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

Go to Cloned (commentary) Search

partial

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

gene gaaB, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae

top print hide References Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Yuen, R.; Schachter, H.

L-Fucose metabolism in mammals. I. Port liver L-fuconate hydro-lyase

Can. J. Biochem.

798-806

1972

Sus scrofa

5050937

brenda

33952

Chan, J.Y.; Nwokoro, N.A.; Schachter, H.

L-Fucose metabolism in mammals. The conversion of L-fucose to two moles of L-lactate, of L-galactose to L-lactate and glycerate, and of D-arabinose to L-lactate and glycollate

J. Biol. Chem.

254

7060-7068

1979

Sus scrofa

457669

brenda

Veiga, L.A.; Guimaes, M.F.

L.Fuconate dehydratase: purification and properties of the enzyme from Pullularia pullulans

Arq. Biol. Tecnol.

537-553

1991

Aureobasidium pullulans

brenda

Yew, W.S.; Fedorov, A.A.; Fedorov, E.V.; Rakus, J.F.; Pierce, R.W.; Almo, S.C.; Gerlt, J.A.

Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris

Biochemistry

14582-14597

2006

Xanthomonas campestris

17144652

brenda