scholarly journals Albucidin: a novel bleaching herbicide from Streptomyces albus subsp. chlorinus NRRL B-24108

2009 ◽  
Vol 62 (4) ◽  
pp. 191-194 ◽  
Author(s):  
Donald R Hahn ◽  
Paul R Graupner ◽  
Eleanor Chapin ◽  
John Gray ◽  
D Heim ◽  
...  
Keyword(s):  
Streptomyces Albus ◽  
Bleaching Herbicide

ChemInform Abstract: Albucidin: A Novel Bleaching Herbicide from Streptomyces albus subsp. chlorinus NRRL B-24108.

ChemInform ◽  
2009 ◽  
Vol 40 (37) ◽  
Author(s):  
Donald R. Hahn ◽  
Paul R. Graupner ◽  
Eleanor Chapin ◽  
John Gray ◽  
D. Heim ◽  
...  
Keyword(s):  
Streptomyces Albus ◽  
Bleaching Herbicide

Transposon-based screen identifies a XRE family regulator crucial for candicidin biosynthesis in Streptomyces albus J1074

2020 ◽  
Vol 63 (9) ◽  
pp. 1-4
Author(s):  
Jun Tian ◽  
Leixin Ye ◽  
Yuling Yang ◽  
Yalin Zhang ◽  
Changhua Hu ◽  
...  
Keyword(s):  
Streptomyces Albus ◽  
Streptomyces Albus J1074

scholarly journals Synthesis of (3Z,6E)-1-N-methylalbonoursin, a new metabolite from Streptomyces albus.

1987 ◽  
Vol 51 (7) ◽  
pp. 2033-2034 ◽  
Author(s):  
Chung-gi SHIN ◽  
Yasuchika YONEZAWA ◽  
Hideki OHNO
Keyword(s):  
Streptomyces Albus

scholarly journals Active-site serine mutants of the Streptomyces albus G β-lactamase

1991 ◽  
Vol 277 (3) ◽  
pp. 647-652 ◽  
Author(s):  
F Jacob ◽  
B Joris ◽  
J M Frère
Keyword(s):  
Active Site ◽  
Specific Activity ◽  
Site Directed Mutagenesis ◽  
Beta Lactamase ◽  
Wild Type ◽  
Serine Residue ◽  
Wild Type Enzyme ◽  
Ph Values ◽  
Streptomyces Albus ◽  
Small Production

By using site-directed mutagenesis, the active-site serine residue of the Streptomyces albus G beta-lactamase was substituted by alanine and cysteine. Both mutant enzymes were produced in Streptomyces lividans and purified to homogeneity. The cysteine beta-lactamase exhibited a substrate-specificity profile distinct from that of the wild-type enzyme, and its kcat./Km values at pH 7 were never higher than 0.1% of that of the serine enzyme. Unlike the wild-type enzyme, the activity of the mutant increased at acidic pH values. Surprisingly, the alanine mutant exhibited a weak but specific activity for benzylpenicillin and ampicillin. In addition, a very small production of wild-type enzyme, probably due to mistranslation, was detected, but that activity could be selectively eliminated. Both mutant enzymes were nearly as thermostable as the wild-type.

scholarly journals THE LYSIS OF GROUP A HEMOLYTIC STREPTOCOCCI BY EXTRACELLULAR ENZYMES OF STREPTOMYCES ALBUS

1952 ◽  
Vol 96 (6) ◽  
pp. 569-580 ◽  
Author(s):  
Maclyn McCarty
Keyword(s):  
Cell Wall ◽  
Extracellular Enzymes ◽  
Group A Streptococci ◽  
Carbohydrate Component ◽  
Streptococcal Cell Wall ◽  
Intact Cells ◽  
Enzymatic Lysis ◽  
Streptomyces Albus ◽  
Group A ◽  
Isolated Cell

Cell wall preparations of uniform chemical constitution have been obtained from several strains of group A streptococci. The isolated cell walls are dissolved by the same fractions of the Streptomyces albus enzymes that are effective in the lysis of intact cells, and it is likely that enzymatic lysis of group A streptococci is effected by an attack on the cell wall. The streptococcal cell wall, as prepared in this study, consists of approximately two-thirds carbohydrate and one-third protein. Small amounts of other components may be present. The carbohydrate component, which is composed primarily of N-acetyl-glucosamine and rhamnose, is the group-specific C carbohydrate. The evidence indicates that one of the streptomyces enzymes is directed toward the carbohydrate component of the cell wall.

scholarly journals Interaction between non-classical β-lactam compounds and the Zn2+-containing G and serine R61 and R39 d-alanyl-d-alanine peptidases

1981 ◽  
Vol 199 (1) ◽  
pp. 129-136 ◽  
Author(s):  
J A Kelly ◽  
J M Frère ◽  
D Klein ◽  
J M Ghuysen
Keyword(s):  
Degradation Products ◽  
The Other ◽  
Reversible Inhibitor ◽  
Beta Lactam ◽  
Beta Lactam Antibiotics ◽  
Streptomyces Albus ◽  
Penicillanic Acid

Streptomyces albus G secretes a Zn2+-containing D-alanyl-D-alanine peptidase. Streptomyces R61 and Actinomadura R39 secrete D-alanyl-D-alanine-cleaving serine peptidases. The effect of non-classical beta-lactam antibiotics on these three model enzymes has been studied. Mecillinam, cefoxitin, quinacillin, quinacillin sulphone, clavulanate and N-formimidoylthienamycin have no effect on the Zn2+-containing enzyme. 6-Amino-penicillanic acid slowly inactivates this enzyme and 7-aminocephalosporanic acid behaves as a reversible inhibitor. Cefoxitin and N-formimidoylthienamycin are potent anti-bacterial agents; they effectively inactivate the serine R39 enzyme and, to a lesser extent, the serine R61 enzyme. All the other beta-lactam compounds tested, including mecillinam, are slow inactivators of these serine enzymes. The intermediates formed between 6-aminopenicillanic acid and the R61 and R39 enzymes are long- and short-lived respectively, whereas those formed between 7-aminocephalosporanic acid and the same R61 and R39 enzymes are short- and long-lived respectively. Breakdown of the short-lived intermediates thus obtained gives rise to several ninhydrin-positive degradation products. The intermediates formed between clavulanate and the serine enzymes are long-lived. With the R39 enzyme, the inactivated complex formed in a first step undergoes subsequent monomolecular rearrangement to give rise to a second species exhibiting a high absorbance at 273 nm.

Sign in / Sign up

Export Citation Format

Share Document