1957
DOI: 10.1128/jb.74.5.646-655.1957
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A NEW SPECIES ( FLAVOBACTERIUM POLYGLUTAMICUM ) WHICH HYDROLYZES THE γ- l -GLUTAMYL BOND IN POLYPEPTIDES

Abstract: It has been shown (Kovacs and Bruckner, 1952; Bruckner et al., 1953a, 1953b, 1953c) that certain bacteria produce glutamyl polypeptides in which the y-glutamyl bond predominates; that produced by Bacillus anthracis (Ivainovics and Erd6s, 1937; Ivanovics and Bruckner, 1937; Hanby and Rydon, 1946) and by Bacillus mesentericus (Bruckner and Ivdnovics, 1937) contains the D-isomer alone, whereas that formed by Bacillus subtilis (Bovarnick, 1942) contains both D-and L-isomers in varying quantities (Thorne et al., 19… Show more

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Cited by 37 publications
(5 citation statements)
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“…and Myrothecium sp. γ‐glutamylhydrolases cleave PGA between two l ‐glutamates (Volcani and Margalith, 1957; Tanaka et al ., 1993; 1997). Finally, the B. subtilis γ‐glutamylhydrolase encoded by pgsS , previously known as ywtD or pgdS , cleaves PGA between two d ‐glutamates (Ashiuchi et al ., 2003).…”
Section: Anchored or Released?mentioning
confidence: 99%
“…and Myrothecium sp. γ‐glutamylhydrolases cleave PGA between two l ‐glutamates (Volcani and Margalith, 1957; Tanaka et al ., 1993; 1997). Finally, the B. subtilis γ‐glutamylhydrolase encoded by pgsS , previously known as ywtD or pgdS , cleaves PGA between two d ‐glutamates (Ashiuchi et al ., 2003).…”
Section: Anchored or Released?mentioning
confidence: 99%
“…The last enzymatic activity that should be mentioned was the first γ-PGA degrading exoenzyme that was characterized; Volcani and Margalith identified an intracellular enzyme activity in the soluble fraction of crude extract prepared from Flavobacterium polyglutamicum cells . The extract hydrolyzed γ- d / l -PGA only in the γ- l -glutamic acid rich regions but completely degraded γ- l -PGA to free l -glutamic acid, which was identified by paper chromatography and manometric determination employing the glutamic acid decarboxylase reaction.…”
Section: Poly-γ-glutamic Acidmentioning
confidence: 99%
“…The extract hydrolyzed γ- d / l -PGA only in the γ- l -glutamic acid rich regions but completely degraded γ- l -PGA to free l -glutamic acid, which was identified by paper chromatography and manometric determination employing the glutamic acid decarboxylase reaction. The remaining γ- d -PGA containing oligomers of the polymer chain were not identified …”
Section: Poly-γ-glutamic Acidmentioning
confidence: 99%
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“…on September 1, 2020 by guest http://jb.asm.org/ Downloaded from 512 ALBRECHT, BOLDIZSAR, AND HUTCHISON Hydrolysis of teropterin (pteroyl--y,-y-triglutamate) to diopterin (pteroyldiglutamate) and partial cleavage of -y-L-glutamyl-L-glutamic acid possibly reflect the presence of a contaminating enzyme (29) or, in fact, limited activity of the carboxypeptidase per se with -y-L-glutamyl-Lglutamic acid. Similarly, the presence of a peptidase specific for the aspartyl moiety (20) or non-specificity of the Flavobacterium sp.…”
Section: Vol 134 1978mentioning
confidence: 99%