Phosphorylation of Streptomycin at C6-OH of Streptidine Moiety by an Intracellular Enzyme of Streptomyces griseus

Nimi, Osamu; Ito, Gaku; Sueda, Satoru; Nomi, Ryosaku

doi:10.1271/bbb1961.35.848

Cited by 11 publications

(2 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Enzymes that modify other antibiotics have been isolated from Streptomyces species; in studies on the biosynthesis of streptomycin in Streptomyces bikiniensis, Miller and Walker (3,8) and Nimi and coworkers (9,10) found three enzymes that phosphorylated streptomycin. In addition, Argoudelis and Coats have reported the presence of enzymes that phosphorylate lincomycin and clindamycin (11), adenylylate clindamycin (12), and acetylate chloramphenicol (13).…”

mentioning

confidence: 99%

Aminoglycoside Antibiotic-Inactivating Enzymes in Actinomycetes Similar to Those Present in Clinical Isolates of Antibiotic-Resistant Bacteria

Benveniste

Davies

1973

Proc. Natl. Acad. Sci. U.S.A.

449

231

View full text Add to dashboard Cite

Various species of Streptomyces possess aminoglycoside-modifying enzymes. Streptomyces kanamyceticus contains an enzyme that acetylates the 6'-amino group of kanamycin A and B, gentamicin Cla, and neomycin. Streptomyces spectabilis produces an enzyme that acetylates the 2'-amino group of the hexose ring of gentamicin Cia. These enzymes catalyze reactions identical to those catalyzed by enzymes found in gram-negative bacteria containing R(antibiotic resistance)-factors. The discovery of these enzymes suggests the possibility of an evolutionary relationship between the aminoglycosideinactivating enzymes (produced by resistance determinants) in bacteria containing R-factors and similar enzymes found in the actinomycetes.Resistance to antibiotics in clinical isolates of gram-negative and gram-positive bacteria is usually mediated by the presence of various enzymes that modify the antibiotic so that it can no longer interact with its target in the cell. The f3-lactamases hydrolyze the penicillins and cephalosporins, chloramphenicol acetyltransferase acetylates chloramphenicol, and nine enzymes acetylate, phosphorylate, or adenylylate the aminoglycoside antibiotics (1, 2). The genetic loci coding for these enzymes are usually located on extrachromosomal elements, such as the R(antibiotic resistance)-factors in gram-negative bacteria. Since these genes are not normal chromosomal components of the resistant strains, there has been considerable speculation as to their origin. Walker and Walker (3) have suggested that some R-factors might have originated in organisms that produce antibiotics.Molecular studies have shown that R-factors consist of two parts that are reversibly dissociable, these are the resistance transfer factor (RTF), and the r-determinants, genes that determine resistance to antibiotics (2). Watanabe (4) has suggested that the r-determinants exist somewhere in nature as chromosomal genes and that they are "picked-up" by promiscuous RTFs to form R-factors. The question is, where do the r-determinants originate?We have initiated a search in the actinomycetes for aminoglycoside-modifying enzymes like those that have been characterized in strains carrying R-factors (R+) in the belief that this might represent the r-determinant gene pool. their cellular dimensions, their cytology, and their genetics place them among the bacteria (5, 6). One of the most striking properties of the actinomycetes is the extent to which they produce antibiotics; most of the aminoglycoside antibiotics (streptomycin, neomycin, kanamycin, gentamicin, tobramycin, and lividomycin) are produced by them.Enzymes that modify other antibiotics have been isolated from Streptomyces species; in studies on the biosynthesis of streptomycin in Streptomyces bikiniensis, Miller and Walker (3,8) and Nimi and coworkers (9, 10) found three enzymes that phosphorylated streptomycin. In addition, Argoudelis and Coats have reported the presence of enzymes that phosphorylate lincomycin and clindamycin (11), adenylylate clindamycin (12), and acetyl...

show abstract

mentioning

confidence: 99%

Aminoglycoside Antibiotic-Inactivating Enzymes in Actinomycetes Similar to Those Present in Clinical Isolates of Antibiotic-Resistant Bacteria

Benveniste

Davies

1973

Proc. Natl. Acad. Sci. U.S.A.

449

231

View full text Add to dashboard Cite

show abstract

“…To date, aminoglycoside O-phosphorylating and N-acetylating enzymes (2), aminocyclitol O-phosphorylating enzymes (3)(4)(5)(6) and chloramphenicol acetyltransferase (EC 2.3.1.28) (7,8) have been detected in antibiotic-producing strains; these enzymes have substrate ranges similar to the plasmid-mediated enzymes found in various Gram-positive and Gram-negative bacteria. It has been suggested, therefore, that antibiotic-producing organisms might represent the origin of r-determinants (2)(3).…”

mentioning

confidence: 99%

Aminoglycoside-modifying enzyme of an antibiotic-producing bacterium acts as a determinant of antibiotic resistance in Escherichia coli.

Courvalin¹,

Weisblum²,

Davies³

1977

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Plasmid-determined antibiotic resistance is widespread in clinical isolates of bacteria. Most determinants of resistance (r-determinants) have no homology with the chromosomal genes of their hosts and Watanabe (1) has suggested that rdeterminants exist "somewhere" in nature as a reservoir of chromosomal genes and that, under the appropriate selection pressures, they were "picked-up" by promiscuous sex factors and, directly or indirectly, transferred to their present hosts.It has been demonstrated (2-8) that many antibiotic-producing bacteria contain antibiotic-modifying enzymes that are related to those that determine antibiotic resistance in plasmid-containing bacteria. To date, aminoglycoside O-phosphorylating and N-acetylating enzymes (2), aminocyclitol O-phosphorylating enzymes (3-6) and chloramphenicol acetyltransferase (EC 2.3.1.28) (7, 8) have been detected in antibiotic-producing strains; these enzymes have substrate ranges similar to the plasmid-mediated enzymes found in various Gram-positive and Gram-negative bacteria. It has been suggested, therefore, that antibiotic-producing organisms might represent the origin of r-determinants (2-3).Support for this notion would come from the demonstration of protein or nucleic acid relationships between antibioticproducing organisms and plasmid-containing antibiotic-resistant bacteria. One can also ask if a gene coding for antibioticmodification in an antibiotic-producing organism could be transplanted to unrelated bacteria such as Escherichia coli; and whether or not this gene would determine antibiotic resistance in the latter.

show abstract

Avoidance of suicide in antibiotic-producing microbes

Cundliffe

Demain

2010

J Ind Microbiol Biotechnol

View full text Add to dashboard Cite

Many microbes synthesize potentially autotoxic antibiotics, mainly as secondary metabolites, against which they need to protect themselves. This is done in various ways, ranging from target-based strategies (i.e. modification of normal drug receptors or de novo synthesis of the latter in drug-resistant form) to the adoption of metabolic shielding and/or efflux strategies that prevent drug-target interactions. These self-defence mechanisms have been studied most intensively in antibiotic-producing prokaryotes, of which the most prolific are the actinomycetes. Only a few documented examples pertain to lower eukaryotes while higher organisms have hardly been addressed in this context. Thus, many plant alkaloids, variously described as herbivore repellents or nitrogen excretion devices, are truly antibiotics-even if toxic to humans. As just one example, bulbs of Narcissus spp. (including the King Alfred daffodil) accumulate narciclasine that binds to the larger subunit of the eukaryotic ribosome and inhibits peptide bond formation. However, ribosomes in the Amaryllidaceae have not been tested for possible resistance to narciclasine and other alkaloids. Clearly, the prevalence of suicide avoidance is likely to extend well beyond the remit of the present article.

show abstract

Phosphorylation of Streptomycin at C6-OH of Streptidine Moiety by an Intracellular Enzyme of Streptomyces griseus

Cited by 11 publications

References 0 publications

Aminoglycoside Antibiotic-Inactivating Enzymes in Actinomycetes Similar to Those Present in Clinical Isolates of Antibiotic-Resistant Bacteria

Aminoglycoside Antibiotic-Inactivating Enzymes in Actinomycetes Similar to Those Present in Clinical Isolates of Antibiotic-Resistant Bacteria

Aminoglycoside-modifying enzyme of an antibiotic-producing bacterium acts as a determinant of antibiotic resistance in Escherichia coli.

Avoidance of suicide in antibiotic-producing microbes

Contact Info

Product

Resources

About