A new dehydrogenase specific towards aromatic aldehydes from a halophilic bacterium.
A new enzyme showing a dehydrogenase activity towards aromatic aldehydes was isolated, purified and characterized from a halophilic strain isolated from saline environment. The enzyme is a monomer of 54 kDa; it is rather thermostable (optimal temperature: 50 degrees C) showing a broad spectrum of activity in a large pH range with the maximum at pH 9.5. The substrate specificity and the effect of ions were evaluated and compared with analogous described proteins.
La Cara
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F
Institute of Protein Biochemistry-C.N.R., Via P. Castellino, 111, 80131, Naples, Italy.
Alves
L
L
Gírio
F
F
Di Salle
A
A
Capasso
A
A
Rossi
M
M
D000444:Aldehyde Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000447:Aldehydes / Q000737:chemistry / Q000378:metabolism*; D004789:Enzyme Activation; D004795:Enzyme Stability; D006216:Halobacteriaceae / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000737:chemistry; D008970:Molecular Weight; D012965:Sodium Chloride / Q000737:chemistry; D013379:Substrate Specificity; D013696:Temperature
D000447:Aldehydes; D008670:Metals; D012965:Sodium Chloride; D000444:Aldehyde Dehydrogenase