Information on EC 4.2.1.25 - L-Arabinonate dehydratase

for references in articles please use BRENDA:EC4.2.1.25
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
4.2.1.25
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RECOMMENDED NAME
GeneOntology No.
L-Arabinonate dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-Arabinonate = 2-dehydro-3-deoxy-L-arabinonate + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-arabinose degradation III
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L-arabinose degradation IV
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degradation of pentoses
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Ascorbate and aldarate metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
L-arabinonate hydro-lyase (2-dehydro-3-deoxy-L-arabinonate-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-30-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MNF300
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Manually annotated by BRENDA team
NGR234
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Manually annotated by BRENDA team
NGR234
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Arabinonate
2-Dehydro-3-deoxy-L-arabinonate
show the reaction diagram
L-Arabinonate
?
show the reaction diagram
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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
L-Arabinonate
?
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
the enzyme contains a [4Fe-4S]2+ cluster
Mg2+
optimal concentration: 1-10 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
2 * 62000, SDS-PAGE
128000
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 62000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant enzymes C47A, C56A, C124A, C197A, and C441A overexpressed in Escherichia coli cells as a His6-tagged enzymes
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C124A
non-colored inactive mutant enzyme, the UV visible absorption spectrum contained no characteristic element of [4Fe-4S]2+
C197A
non-colored inactive mutant enzyme, the UV visible absorption spectrum contained no characteristic element of [4Fe-4S]2+
C441A
brown-colored mutant is significantly active and UV-visible absorption spectrum is similar to those of the wild-type enzyme
C47A
brown-colored mutant is significantly active and UV-visible absorption spectrum is similar to those of the wild-type enzyme
C56A
inactive mutant partiall shares similar behavior to the wild-type in color and UV-visible absorption spectrum
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Show AA Sequence (325 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.1.25)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)