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In Escherichia coli, the ATP-bound form of DnaA (ATP-DnaA) promotes replication initiation. During replication, the bound ATP is hydrolyzed to ADP to yield the ADP-bound form (ADP-DnaA), which is inactive for initiation. The chromosomal site DARS2 facilitates the regeneration of ATP-DnaA by catalyzing nucleotide exchange between free ATP and ADP bound to(More)
The substrate specificities of two different molecular sizes of cathepsin A, A,L (large form) and A,S (small form), for synthetic substrates were examined kinetically. Both enzymes showed a similar broad substrate specificity against various acyl dipeptides, amino acid esters, and amino acid amides. Z-Phe-Ala and Ac-Phe-OEt were good substrates. Peptides(More)
The two forms of pig kidney cathepsin A (A,L and A,S) were found to be composed of three kinds of polypeptides as common structural subunits with molecular weights of 20,000, 25,000, and 55,000. [32P]-DFP was incorporated into the subunit with a molecular weight of 25,000. This subunit seems to be a catalytic one, on which active serine is present. A(More)
Cathepsin A [EC 3.4.2.-] of small molecular size (cathepsin A, S) has been purified about 800-fold from pig kidney by procedures including chromatographies on DEAE-Sephadex, SP-Sephadex, and Sephadex G-150. 1. The homogeneity of the purified enzyme was proved by ultracentrifugation and polyacrylamide gel electrophoresis. The molecular weight (100,000) and(More)
The substrate specificity of carboxypeptidase (F-II) purified from watermelon for various synthetic peptides and esters was examined kinetically. The enzyme showed a broad substrate specificity against various carbobenzoxy- and benzyl-dipeptides. Peptides containing glycine or proline were hydrolyzed slowly by the enzyme. Peptides containing hydrophobic(More)
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