[A membrane-bound alanine aminopeptidase from Acinetobacter calcoaceticus. 2. Substrate specificity of the enzyme].
The substrate specificity of the membrane-bound alanine aminopeptidase from Acinetobacter calcoaceticus was investigated with a series of substituted amides of alpha-amino acids. In contrast to mammalian AAP forms, the rate of hydrolysis of the AAP from Acinetobacter calcoaceticus is higher using 4-nitranilide than 2-naphthylamide substrates. The enzyme affinity is very high for alanine substrates and decreases in the series of the amide substituents, from methyl coumarylamides, 4-nitranilides, 4-methoxynaphthylamides to the 2-naphthylamides. The alanine aminopeptidase shows its highest affinity to Ala-MCA (Km = 77 mumol(s)/1).
Jahreis
G
G
Institut für Biochemie, Bereich Medizin, Martin-Luther-Universität Halle-Wittenberg.
Buchholz
A
A
Aurich
H
H
D000150:Acinetobacter / Q000201:enzymology*; D000409:Alanine / Q000378:metabolism; D000626:Aminopeptidases / Q000378:metabolism*; D018826:CD13 Antigens; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008566:Membranes / Q000201:enzymology; D013379:Substrate Specificity; D013696:Temperature
D000626:Aminopeptidases; D018826:CD13 Antigens; D000409:Alanine
Eine membrangebundene Alaninaminopeptidase aus Acinetobacter calcoaceticus. 2. Substratspezifität des Enzyms.