Limits...
Regulation and compartmentalization of β-lactam biosynthesis.

Martín JF, Ullán RV, García-Estrada C - Microb Biotechnol (2009)

Bottom Line: Similarly, the Acremonium two-component CefD1-CefD2 epimerization system is also located in microbodies.This compartmentalization implies intracellular transport of isopenicillin N (in the penicillin pathway) or isopenicillin N and penicillin N in the cephalosporin route.Two transporters of the MFS family cefT and cefM are involved in transport of intermediates and/or secretion of cephalosporins.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biotechnology of León, Science Park, Avda. Real 1, 24006 León, Spain. jf.martin@unileon.es

Show MeSH

Related in: MedlinePlus

Proposed model describing the compartmentalization of the cephalosporin C biosynthetic pathway in A. chrysogenum showing the localization of the CefT and CefM transporters. ACVS, δ‐l‐α‐aminoadipyl‐l‐cysteinyl‐d‐valine synthetase; ACV, l‐δ(α‐aminoadipyl)‐l‐cysteinyl‐d‐valine; IPNS isopenicillin N synthase; IPN, isopenicillin N; IPN‐ACS isopenicillin N‐CoA synthetase; IPN‐ACE; isopenicillin N‐CoA epimerase; PenN, penicillin N; EH, deacetoxycephalosporin synthase (expandase/hydroxylase); DAC, deacetylcephalosporin C; DAC‐AT, deacetylcephalosporin acetyltransferase; CPC, cephalosporin C.
© Copyright Policy
Related In: Results  -  Collection


getmorefigures.php?uid=PMC3815371&req=5

f5: Proposed model describing the compartmentalization of the cephalosporin C biosynthetic pathway in A. chrysogenum showing the localization of the CefT and CefM transporters. ACVS, δ‐l‐α‐aminoadipyl‐l‐cysteinyl‐d‐valine synthetase; ACV, l‐δ(α‐aminoadipyl)‐l‐cysteinyl‐d‐valine; IPNS isopenicillin N synthase; IPN, isopenicillin N; IPN‐ACS isopenicillin N‐CoA synthetase; IPN‐ACE; isopenicillin N‐CoA epimerase; PenN, penicillin N; EH, deacetoxycephalosporin synthase (expandase/hydroxylase); DAC, deacetylcephalosporin C; DAC‐AT, deacetylcephalosporin acetyltransferase; CPC, cephalosporin C.

Mentions: Based on these results, we propose a hypothetical model of compartmentalization in the biosynthesis of cephalosporins (Fig. 5). This compartmentalization model starts with the ACV and IPN synthesis in the cytosol by cytoplasmic ACV synthetase and IPN synthase (Evers et al., 2004). Later the IPN is transported to the peroxisome where it is converted in PenN by the two‐protein (CefD1–CefD2) epimerization system (Ullán et al., 2002a). Afterwards, the penicillin N is transported to the cytosol, by means of the CefM carrier (Teijeira et al., 2009), where the two last enzymes of the cephalosporin pathway synthesize cephalosporin C (van de Kamp et al., 1999; Evers et al., 2004). On the other hand, the secretion of intermediates of the cephalosporin C biosynthetic pathway in A. chrysogenum appears to be performed by the CefT trasporter (Fig. 5). Although the CefT protein has not been yet localized in A. chrysogenum using fluorescent dyes, heterologous expression of the CefT–GFP fusion in P. chrysogenum indicates that it is located in the plasma membrane (Nijland et al., 2008).


Regulation and compartmentalization of β-lactam biosynthesis.

Martín JF, Ullán RV, García-Estrada C - Microb Biotechnol (2009)

Proposed model describing the compartmentalization of the cephalosporin C biosynthetic pathway in A. chrysogenum showing the localization of the CefT and CefM transporters. ACVS, δ‐l‐α‐aminoadipyl‐l‐cysteinyl‐d‐valine synthetase; ACV, l‐δ(α‐aminoadipyl)‐l‐cysteinyl‐d‐valine; IPNS isopenicillin N synthase; IPN, isopenicillin N; IPN‐ACS isopenicillin N‐CoA synthetase; IPN‐ACE; isopenicillin N‐CoA epimerase; PenN, penicillin N; EH, deacetoxycephalosporin synthase (expandase/hydroxylase); DAC, deacetylcephalosporin C; DAC‐AT, deacetylcephalosporin acetyltransferase; CPC, cephalosporin C.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3815371&req=5

f5: Proposed model describing the compartmentalization of the cephalosporin C biosynthetic pathway in A. chrysogenum showing the localization of the CefT and CefM transporters. ACVS, δ‐l‐α‐aminoadipyl‐l‐cysteinyl‐d‐valine synthetase; ACV, l‐δ(α‐aminoadipyl)‐l‐cysteinyl‐d‐valine; IPNS isopenicillin N synthase; IPN, isopenicillin N; IPN‐ACS isopenicillin N‐CoA synthetase; IPN‐ACE; isopenicillin N‐CoA epimerase; PenN, penicillin N; EH, deacetoxycephalosporin synthase (expandase/hydroxylase); DAC, deacetylcephalosporin C; DAC‐AT, deacetylcephalosporin acetyltransferase; CPC, cephalosporin C.
Mentions: Based on these results, we propose a hypothetical model of compartmentalization in the biosynthesis of cephalosporins (Fig. 5). This compartmentalization model starts with the ACV and IPN synthesis in the cytosol by cytoplasmic ACV synthetase and IPN synthase (Evers et al., 2004). Later the IPN is transported to the peroxisome where it is converted in PenN by the two‐protein (CefD1–CefD2) epimerization system (Ullán et al., 2002a). Afterwards, the penicillin N is transported to the cytosol, by means of the CefM carrier (Teijeira et al., 2009), where the two last enzymes of the cephalosporin pathway synthesize cephalosporin C (van de Kamp et al., 1999; Evers et al., 2004). On the other hand, the secretion of intermediates of the cephalosporin C biosynthetic pathway in A. chrysogenum appears to be performed by the CefT trasporter (Fig. 5). Although the CefT protein has not been yet localized in A. chrysogenum using fluorescent dyes, heterologous expression of the CefT–GFP fusion in P. chrysogenum indicates that it is located in the plasma membrane (Nijland et al., 2008).

Bottom Line: Similarly, the Acremonium two-component CefD1-CefD2 epimerization system is also located in microbodies.This compartmentalization implies intracellular transport of isopenicillin N (in the penicillin pathway) or isopenicillin N and penicillin N in the cephalosporin route.Two transporters of the MFS family cefT and cefM are involved in transport of intermediates and/or secretion of cephalosporins.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biotechnology of León, Science Park, Avda. Real 1, 24006 León, Spain. jf.martin@unileon.es

Show MeSH
Related in: MedlinePlus