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Information on EC 4.2.1.7 - altronate dehydratase
for references in articles please use BRENDA:EC4.2.1.7
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The enzyme appears in viruses and cellular organisms
showSynonyms
ACAV_RS08155, Altronic acid hydratase, D-altronate dehydratase, dehydratase, altronate, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACAV_RS08155
Altronic acid hydratase
-
-
-
-
D-altronate dehydratase
dehydratase, altronate
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-altronate = 2-dehydro-3-deoxy-D-gluconate + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
D-galacturonate degradation I
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SYSTEMATIC NAME
IUBMB Comments
D-altronate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
62213-26-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-altronate
?
-
Substrates: the enzyme is involved in the galacturonate branch of the hexuronate pathway
Products: -
Products: -
?
L-gluconate
2-dehydro-3-deoxy-L-gluconate + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with L-galactonate
Products: -
Products: -
-
D-altronate
2-dehydro-3-deoxy-D-gluconate + H2O
-
Substrates: -
Products: -
Products: -
?
D-altronate
2-dehydro-3-deoxy-D-gluconate + H2O
-
Substrates: -
Products: -
Products: -
ir
D-altronate
2-dehydro-3-deoxy-D-gluconate + H2O
-
Substrates: -
Products: -
Products: -
?
D-altronate
2-dehydro-3-deoxy-D-gluconate + H2O
-
Substrates: -
Products: -
Products: -
?
D-arabinonate
2-dehydro-3-deoxy-D-arabinonate + H2O
-
Substrates: -
Products: -
Products: -
r
D-arabinonate
2-dehydro-3-deoxy-D-arabinonate + H2O
-
Substrates: -
Products: -
Products: -
r
D-idonate
2-dehydro-3-deoxy-D-galactonate + H2O
-
Substrates: -
Products: -
Products: -
?
D-idonate
2-dehydro-3-deoxy-D-galactonate + H2O
-
Substrates: -
Products: -
Products: -
?
L-fuconate
2-dehydro-3-deoxy-L-fuconate + H2O
-
Substrates: -
Products: -
Products: -
?
L-fuconate
2-dehydro-3-deoxy-L-fuconate + H2O
-
Substrates: -
Products: -
Products: -
?
L-xylonate
2-dehydro-3-deoxy-L-pentonate + H2O
-
Substrates: -
Products: -
Products: -
?
L-xylonate
2-dehydro-3-deoxy-L-pentonate + H2O
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-altronate
?
-
Substrates: the enzyme is involved in the galacturonate branch of the hexuronate pathway
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mn2+
-
activates, synergistic activation in presence of both, Mg2+ and Mn2+. Mn2+ appears to be a constituent of the enzyme active center
Fe2+
-
low concentrations required, inhibition above 2 mM. Upon activation the enzyme incorporates a single Fe atom. The incorporated iron is losely bound. Synergistic activation in presence of both, Mg2+ and Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
sulfhydryl compounds required, 50 mM 2-mercaptoethanol in presence of 0.8 mM FeSO4 is optimal
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of high concentrations, 0.1 M, of Cys or mercaptoethanol and maintenance in pH range pH 7.0-8.0 stabilizes throughout purification
-
freezing, agitation or stirring in the presence of air or dialysis at pH levels below pH 7.0 inactivates
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Robert-Baudouy, J.; Jimeno-Abendano, J.; Stoeber, F.
D-Mannonate and D-altronate dehydratases of Escherichia coli K12
Methods Enzymol.
90
288-294
1982
Escherichia coli
brenda
Dreyer, J.L.
The role of iron in the activation of mannonic and altronic acid hydratases, two Fe-requiring hydro-lyases
Eur. J. Biochem.
166
623-630
1987
Escherichia coli
brenda
Smiley, J.D.; Ashwell, G.
Uronic acid metabolism in bacteria. III. Purification and properties of D-altronic acid and D-mannonic acid dehydrases in Escherichia coli
J. Biol. Chem.
235
1571-1575
1960
Escherichia coli
brenda
Watanabe, S.; Fukumori, F.; Watanabe, Y.
Substrate and metabolic promiscuities of D-altronate dehydratase family proteins involved in non-phosphorylative D-arabinose, sugar acid, L-galactose and L-fucose pathways from bacteria
Mol. Microbiol.
112
147-165
2019
Paracidovorax avenae, Paracidovorax avenae ATCC 19860
brenda
EXTERNAL LINKS (specific for EC-Number 4.2.1.7)
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Release 2026.1 (March 2026)
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