[29] δ-(α-Aminoadipyl)cysteinylvaline synthetase

Fawcett, Patricia; Abraham, E. P.

doi:10.1016/0076-6879(75)43105-6

Cited by 24 publications

(12 citation statements)

References 6 publications

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“…They provided evidence that during cell fractionation, ACV-synthetase sediments with a 100000 g fraction, whose origin has not yet been characterized. A membrane-associated ACVsynthetase was also apparent from earlier studies (Fawcett & Abraham, 1975). Binding of ACV-synthetase to a compartment containing the precursor amino acids for penicillin biosynthesis would explain the observed differences in 4C-valine incorporation into protein and penicillin, although we cannot deduce any information on the identity of this compartment from our results.…”

Section: Discussioncontrasting

confidence: 42%

Evidence for a compartmentation of penicillin biosynthesis in a high- and a low-producing strain of Penicillium chrysogenum

Affenzeller

Kubicek

1991

Journal of General Microbiology

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Pulse-chase experiments using (U14C]valine were done with P2 and 4176, high-and low-penicillin-producing strains of Penicillium chrysogenum. The metabolic flux of this amino acid into protein and penicillin was measured, and compartmentation of penicillin biosynthesis was assessed. Strain P2 took up 14C-valine more slowly than strain Q176, but their rates of incorporation into protein were comparable. Incorporation of 14C-valine into penicillin occurred immediately with the high-producer P2, but exhibited a lag with Q176. After 14C-valine had been removed from the medium, the specific radioactivity of penicillin continued to increase in 4176 but started to decrease immediately in P2. The specific radioactivities of 4C-valine in protein and in penicillin were significantly different in both strains: Q176 had a higher specific radioactivity of valine in penicillin than P2, whereas P2 had a higher specific radioactivity of valine in protein than 4176. Moreover, the specific radioactivity of 14C-valine in penicillin was 20-fold higher in strain 4176 than in P2. These results indicate that penicillin and protein biosynthesis use different pools of cellular valine, and that exchange of valine between the two compartments is slow in the low-producer, but rapid in the high-producer strain. Hence these results indicate a further control point of penicillin biosynthesis in P. chrysogenum.

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Section: Discussioncontrasting

confidence: 42%

Evidence for a compartmentation of penicillin biosynthesis in a high- and a low-producing strain of Penicillium chrysogenum

Affenzeller

Kubicek

1991

Journal of General Microbiology

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“…In all species so far investigated, the biosynthesis of penicillin and cephalosporin compounds involves the tripeptide •-(L-a-aminoadipyl)-Lcysteinyl-D-valine (ACV) as an early intermediate. While the enzymatic reaction which converts ACV into the penicillin nucleus has been studied extensively [1][2][3][4], the reaction(s) giving rise to ACV have been much more resistant to analysis [5,6]. Early studies on ACV biosynthesis concentrated on the analogy of the ACV structure with that of glutathione, and searched for similar biosynthetic routes involving two enzymes [7].…”

Section: Introductionmentioning

confidence: 99%

Production of the penicillin precursor Î´-(L-Î±-aminoadipyl)-L-cysteinyl-D-valine (ACV) by cell-free extracts fromStreptomyces clavuligerus

Jensen

Westlake

Wolfe

1988

FEMS Microbiology Letters

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Glycerol‐stabilised cell extracts of Streptomyces clavuligerus contain an enzyme activity which synthesises ACV from the individual amino acids L‐α‐aminoadipic acid, L‐cysteine and L‐valine. Enzyme activity was optimum in reaction mixtures containing 1 mM ATP together with an ATP regenerating system. The ACV synthetase enzyme formed ACV analogs when provided with L‐ carboxymethylcysteine in place of L‐α‐aminoadipic acid or when provided with L‐alloisoleucine or L‐α‐aminobutyrate in place of L‐valine. Multistep conversion of individual amino acids to penicillin and cephalosporin antibiotics was restricted as a result of the inhibitory effects of L‐α‐aminoadipic acid and L‐cysteine on isopenicillin N synthetase.

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“…Furthermore, no LLD-peptide was formed from L-Aad-L-CysH and -valine in cellfree systems of a Cephalosporium sp. (9). One could also assume that the LL-tripeptide is latter compound has not yet been detected in mycelial extracts.…”

mentioning

confidence: 99%

“…Since the chiral center of the valinederived part of penicillin has the D-configuration, it was assumed that inversion occurred at some further step of the biosynthesis. More recently, however, it was shown that the tripeptide of Cephalosporium has the LDconfiguration (9,16). This LuD-peptide is now considered to be a possible precursor of penicillin and cephalosporin (8).…”

mentioning

confidence: 99%

Presence of δ-( l -α-Aminoadipyl)- l -Cysteinyl- d -Valine in Fermentations of Penicillium chrysogenum

Adriaens

Meesschaert

Wuyts

et al. 1975

Antimicrob Agents Chemother

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Cultures of Penicillium chrysogenum , growth with [ 35 S]sulfate or labeled amino acids, were examined by ion-exchange chromatography for possible peptidic precursors of penicillin. A sulfur-containing compound, present in both the mycelial extracts and the culture filtrates, was eluted at the location of the synthetic lld -tripeptide δ-( l -α-aminoadipyl)- l -cysteinyl- d -valine. Since this compound was also labeled when the cultures were incubated with dl -[6- 14 C]α-aminoadipic acid, l -[3,3′- 3 H]cystine, or dl -[1- 14 C]valine, its identity with the synthetic lld -tripeptide can be accepted. No δ-( l -α-aminoadipyl)- l -cysteine or lll -tripeptide were detected. The implications of these findings for tripeptide and penicillin biosynthesis are discussed.

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[29] δ-(α-Aminoadipyl)cysteinylvaline synthetase

Cited by 24 publications

References 6 publications

Evidence for a compartmentation of penicillin biosynthesis in a high- and a low-producing strain of Penicillium chrysogenum

Evidence for a compartmentation of penicillin biosynthesis in a high- and a low-producing strain of Penicillium chrysogenum

Production of the penicillin precursor Î´-(L-Î±-aminoadipyl)-L-cysteinyl-D-valine (ACV) by cell-free extracts fromStreptomyces clavuligerus

Presence of δ-( l -α-Aminoadipyl)- l -Cysteinyl- d -Valine in Fermentations of Penicillium chrysogenum

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