L-arabinonate dehydratase activity

Known as: L-arabonate dehydratase activity, L-arabinonate hydro-lyase activity, L-arabinonate hydro-lyase (2-dehydro-3-deoxy-L-arabinonate-forming) 
Catalysis of the reaction: L-arabinonate = 2-dehydro-3-deoxy-L-arabinonate + H(2)O. [EC:4.2.1.25, RHEA:20971]
National Institutes of Health

Papers overview

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2016
2016
Crystallization and X-ray diffraction analysis of an l-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii and a d-xylonate dehydratase from Caulobacter crescentus
L-Arabinonate dehydratase (EC 4.2.1.25) and D-xylonate dehydratase (EC 4.2.1.82) are two enzymes that are involved in a… (More)
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2014
2014
L-arabonate and D-galactonate production by expressing a versatile sugar dehydrogenase in metabolically engineered Escherichia coli.
The production of L-arabonate and D-galactonate employing a versatile l-arabinose dehydrogenase (AraDH) from Azospirillum… (More)
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2011
2011
Formation of 4-keto-D-aldopentoses and 4-pentulosonates (4-keto-D-pentonates) with unidentified membrane-bound enzymes from acetic acid bacteria.
In our previous study, a new microbial reaction yielding 4-keto-D-arabonate from 2,5-diketo-D-gluconate was identified with… (More)
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2006
2006
L-galactonate dehydratase is part of the fungal path for D-galacturonic acid catabolism.
An L-galactonate dehydratase and the corresponding gene were identified from the mould Hypocrea jecorina (Trichoderma reesei… (More)
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2006
2006
Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris.
Many members of the mechanistically diverse enolase superfamily have unknown functions. In this report we use both genome (operon… (More)
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2006
2006
Identification and characterization of L-arabonate dehydratase, L-2-keto-3-deoxyarabonate dehydratase, and L-arabinolactonase involved in an alternative pathway of L-arabinose metabolism. Novel…
Azospirillum brasiliense possesses an alternative pathway of L-arabinose metabolism, different from the known bacterial and… (More)
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2004
2004
The structures of inhibitor complexes of Pyrococcus furiosus phosphoglucose isomerase provide insights into substrate binding and catalysis.
Pyrococcus furiosus phosphoglucose isomerase (PfPGI) is a metal-containing enzyme that catalyses the interconversion of glucose 6… (More)
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2001
2001
Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonate identifies the role of Glu357 in catalysis.
Phosphoglucose isomerase (PGI; E.C. 5.3.1.9) catalyzes the second step in glycolysis, the interconversion of D-glucose-6… (More)
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1975
1975
L-fucose metabolism in mammals. Purification of pork liver 2-keto-3-deoxy-L-fuconate:NAD+ oxidoreductase by NAD+-Agarose affinity chromatography.
Pork liver has previously been reported to contain a soluble enzymatic pathway which converts L-fucose to 2-keto-3-deoxy-L… (More)
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1975
1975
L-fucose metabolism in mammals. Kinetic studies on pork liver 2-keto-3-deoxy-L-fuconate:NAD+ oxidoreductase.
Pork liver 2-keto-3-deoxy-L-fuconate:NAD+ oxidoreductase has been shown to convert 2-keto-3-deoxy-L-fuconate to a 6-carbon acid… (More)
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