HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Vosbeck, K. D. Articles by Awad, W. M. Search for Related Content PubMed PubMed Citation Articles by Vosbeck, K. D. Articles by Awad, W. M., Jr Social Bookmarking                      What's this?

JBC, Vol. 250, Issue 10, 3981-3987, May, 1975

The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Specificity and immobilization of aminopeptidase

K. D. Vosbeck, B. D. Greenberg and W. M. Awad Jr

We recently described the purification of two aminopeptidases from Streptomyces griseus (Vosbeck, K.D., Chow, K.-F., and Awad, W.M., Jr. (1973) J. Biol. Chem. 248, 6329-6034). An analysis of the amino acid composition reveals very little differences in the two proteins. Each protein has alanine as the NH2-terminal residue. The aminopeptidases were treated separately with acetic anhydride; as noted in the past, the presence of glycerol is required to achieve excellent yields of acetylated active derivatives (Siegel, S., and Awad, W.M., Jr. (1973 J. Biol. Chem. 248, 3233-3240). However, in the present case much higher concentrations of glycerol (50%) are needed during acetylation to obtain derivatives with completely reacted NH2-terminal residues. The epsilon-amino groups were not completely acetylated. In contrast to the native enzymes, the acetylated derivatives show an affinity for DEAE-cellulose, a property consonant with the changes in net charge. The kinetic constants for each enzyme against L-leucine-p-nitroanilide do not change significantly after acetylation. The specificities of the two aminopeptidases were examined extensively on a semiquantitative basis. The activities are not restricted by the length of substrate chains. Each enzyme shows a preference for hydrophobic residues at the ultimate and penultimate positions. Charge residues are released a slower rates. No prolidase activity is demonstrable even at high enzyme to substrate ratios; however, NH2-terminal proline residues are released readily. D-Amino acid residues at the ultimate or penultimate position substantially reduce the rate of hydrolysis; D-leucyl-D-leucine is not hydrolyzed...
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Arima, Y. Uesugi, M. Uraji, S. Yatsushiro, S. Tsuboi, M. Iwabuchi, and T. Hatanaka Modulation of Streptomyces Leucine Aminopeptidase by Calcium: IDENTIFICATION AND FUNCTIONAL ANALYSIS OF KEY RESIDUES IN ACTIVATION AND STABILIZATION BY CALCIUM J. Biol. Chem., March 3, 2006; 281(9): 5885 - 5894. [Abstract] [Full Text] [PDF]

				J. Arima, Y. Uesugi, M. Iwabuchi, and T. Hatanaka Alteration of Leucine Aminopeptidase from Streptomyces septatus TH-2 to Phenylalanine Aminopeptidase by Site-Directed Mutagenesis Appl. Envir. Microbiol., November 1, 2005; 71(11): 7229 - 7235. [Abstract] [Full Text] [PDF]