The Enzyme Database

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EC 1.14.11.26     
Accepted name: deacetoxycephalosporin-C hydroxylase
Reaction: deacetoxycephalosporin C + 2-oxoglutarate + O2 = deacetylcephalosporin C + succinate + CO2
For diagram of cephalosporin biosynthesis, click here
Other name(s): deacetylcephalosporin C synthase; 3′-methylcephem hydroxylase; DACS; DAOC hydroxylase; deacetoxycephalosporin C hydroxylase
Systematic name: deacetoxycephalosporin-C,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires iron(II). The enzyme can also use 3-exomethylenecephalosporin C as a substrate to form deacetoxycephalosporin C, although more slowly [2]. In Acremonium chrysogenum, the enzyme forms part of a bifunctional protein along with EC 1.14.20.1, deactoxycephalosporin-C synthase. It is a separate enzyme in Streptomyces clavuligerus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 69772-89-0
References:
1.  Dotzlaf, J.E. and Yeh, W.K. Copurification and characterization of deacetoxycephalosporin C synthetase/hydroxylase from Cephalosporium acremonium. J. Bacteriol. 169 (1987) 1611–1618. [DOI] [PMID: 3558321]
2.  Baker, B.J., Dotzlaf, J.E. and Yeh, W.K. Deacetoxycephalosporin C hydroxylase of Streptomyces clavuligerus. Purification, characterization, bifunctionality, and evolutionary implication. J. Biol. Chem. 266 (1991) 5087–5093. [PMID: 2002049]
3.  Coque, J.J., Enguita, F.J., Cardoza, R.E., Martin, J.F. and Liras, P. Characterization of the cefF gene of Nocardia lactamdurans encoding a 3′-methylcephem hydroxylase different from the 7-cephem hydroxylase. Appl. Microbiol. Biotechnol. 44 (1996) 605–609. [PMID: 8703431]
4.  Ghag, S.K., Brems, D.N., Hassell, T.C. and Yeh, W.K. Refolding and purification of Cephalosporium acremonium deacetoxycephalosporin C synthetase/hydroxylase from granules of recombinant Escherichia coli. Biotechnol. Appl. Biochem. 24 (1996) 109–119. [PMID: 8865604]
5.  Lloyd, M.D., Lipscomb, S.J., Hewitson, K.S., Hensgens, C.M., Baldwin, J.E. and Schofield, C.J. Controlling the substrate selectivity of deacetoxycephalosporin/deacetylcephalosporin C synthase. J. Biol. Chem. 279 (2004) 15420–15426. [DOI] [PMID: 14734549]
6.  Wu, X.B., Fan, K.Q., Wang, Q.H. and Yang, K.Q. C-terminus mutations of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase with improved activity toward penicillin analogs. FEMS Microbiol. Lett. 246 (2005) 103–110. [DOI] [PMID: 15869968]
7.  Martín, J.F., Gutiérrez, S., Fernández, F.J., Velasco, J., Fierro, F., Marcos, A.T. and Kosalkova, K. Expression of genes and processing of enzymes for the biosynthesis of penicillins and cephalosporins. Antonie Van Leeuwenhoek 65 (1994) 227–243. [PMID: 7847890]
[EC 1.14.11.26 created 2005]
 
 
EC 1.14.20.1     
Accepted name: deacetoxycephalosporin-C synthase
Reaction: penicillin N + 2-oxoglutarate + O2 = deacetoxycephalosporin C + succinate + CO2 + H2O
For diagram of penicillin-N and deacetoxycephalosporin-C biosynthesis, click here
Other name(s): DAOCS; penicillin N expandase; DAOC synthase
Systematic name: penicillin-N,2-oxoglutarate:oxygen oxidoreductase (ring-expanding)
Comments: Forms part of the penicillin biosynthesis pathway (for pathway, click here).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 85746-10-7
References:
1.  Cantwell, C., Beckmann, R., Whiteman, P., Queener, S.W. and Abraham, E.P. Isolation of deacetoxycephalosporin-c from fermentation broths of Penicillium chrysogenum transformants - construction of a new fungal biosynthetic-pathway. Proc. R. Soc. Lond. B Biol. Sci. 248 (1992) 283–289. [DOI] [PMID: 1354366]
2.  Lee, H.J., Lloyd, M.D., Harlos, K., Clifton, I.J., Baldwin, J.E. and Schofield, C.J. Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS). J. Mol. Biol. 308 (2001) 937–948. [DOI] [PMID: 11352583]
3.  Yeh, W.K., Ghag, S.K. and Queener, S.W. Enzymes for epimerization of isopenicillin N, ring expansion of penicillin N, and 3′-hydroxylation of deacetoxycephalosporin C. Function, evolution, refolding, and enzyme engineering. Ann. N.Y. Acad. Sci. 672 (1992) 396–408.
4.  Valegaard, K., van Scheltinga, A.C.T., Lloyd, M.D., Hara, T., Ramaswamy, S., Perrakis, A., Thompson, A., Lee, H.-J., Baldwin, J.E., Schofield, C.J., Hajdu, J. and Andersson, I. Structure of a cephalosporin synthase. Nature 394 (1998) 805–809. [DOI] [PMID: 9723623]
5.  Dotzlaf, J.E. and Yeh, W.K. Purification and properties of deacetoxycephalosporin C synthase from recombinant Escherichia coli and its comparison with the native enzyme purified from Streptomyces clavuligerus. J. Biol. Chem. 264 (1989) 10219–10227. [PMID: 2656705]
[EC 1.14.20.1 created 2002]
 
 
EC 2.3.1.175     
Accepted name: deacetylcephalosporin-C acetyltransferase
Reaction: acetyl-CoA + deacetylcephalosporin C = CoA + cephalosporin C
For diagram of cephalosporin biosynthesis, click here
Other name(s): acetyl-CoA:deacetylcephalosporin-C acetyltransferase; DAC acetyltransferase; cefG; deacetylcephalosporin C acetyltransferase; acetyl coenzyme A:DAC acetyltransferase; acetyl-CoA:DAC acetyltransferase; CPC acetylhydrolase; acetyl-CoA:DAC O-acetyltransferase; DAC-AT
Systematic name: acetyl-CoA:deacetylcephalosporin-C O-acetyltransferase
Comments: This enzyme catalyses the final step in the biosynthesis of cephalosporin C.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 57827-76-6
References:
1.  Matsuyama, K., Matsumoto, H., Matsuda, A., Sugiura, H., Komatsu, K. and Ichikawa, S. Purification of acetyl coenzyme A: deacetylacephalosporin C O-acetyltransferase from Acremonium chrysogenum. Biosci. Biotechnol. Biochem. 56 (1992) 1410–1412. [DOI] [PMID: 1368946]
2.  Gutiérrez, S., Velasco, J., Fernandez, F.J. and Martín, J.F. The cefG gene of Cephalosporium acremonium is linked to the cefEF gene and encodes a deacetylcephalosporin C acetyltransferase closely related to homoserine O-acetyltransferase. J. Bacteriol. 174 (1992) 3056–3064. [DOI] [PMID: 1569032]
3.  Matsuda, A., Sugiura, H., Matsuyama, K., Matsumoto, H., Ichikawa, S. and Komatsu, K. Cloning and disruption of the cefG gene encoding acetyl coenzyme A: deacetylcephalosporin C O-acetyltransferase from Acremonium chrysogenum. Biochem. Biophys. Res. Commun. 186 (1992) 40–46. [DOI] [PMID: 1632779]
4.  Gutiérrez, S., Velasco, J., Marcos, A.T., Fernández, F.J., Fierro, F., Barredo, J.L., Díez, B. and Martín, J.F. Expression of the cefG gene is limiting for cephalosporin biosynthesis in Acremonium chrysogenum. Appl. Microbiol. Biotechnol. 48 (1997) 606–614. [PMID: 9421924]
5.  Velasco, J., Gutierrez, S., Campoy, S. and Martin, J.F. Molecular characterization of the Acremonium chrysogenum cefG gene product: the native deacetylcephalosporin C acetyltransferase is not processed into subunits. Biochem. J. 337 (1999) 379–385. [PMID: 9895280]
6.  Martín, J.F., Gutiérrez, S., Fernández, F.J., Velasco, J., Fierro, F., Marcos, A.T. and Kosalkova, K. Expression of genes and processing of enzymes for the biosynthesis of penicillins and cephalosporins. Antonie Van Leeuwenhoek 65 (1994) 227–243. [PMID: 7847890]
[EC 2.3.1.175 created 2005]
 
 
EC 2.6.1.74     
Accepted name: cephalosporin-C transaminase
Reaction: (7R)-7-(5-carboxy-5-oxopentanoyl)aminocephalosporinate + D-glutamate = cephalosporin C + 2-oxoglutarate
For diagram of cephalosporin biosynthesis, click here
Glossary: cephalosporin C = (7R)-7-(5-carboxy-5-oxopentanamido)cephalosporanate
Other name(s): cephalosporin C aminotransferase; L-alanine:cephalosporin-C aminotransferase
Systematic name: cephalosporin-C:2-oxoglutarate aminotransferase
Comments: A number of D-amino acids, including D-alanine, D-aspartate and D-methionine can also act as amino-group donors. Although this enzyme acts on several free D-amino acids, it differs from EC 2.6.1.21, D-alanine transaminase, in that it can use cephalosporin C as an amino donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122096-91-7
References:
1.  Aretz, W. and Sauber, K. Novel D-amino acid transaminase. Ann. N.Y. Acad. Sci. 542 (1988) 366–370. [PMID: 3228235]
[EC 2.6.1.74 created 1992, modified 2005]
 
 
EC 3.1.1.41     
Accepted name: cephalosporin-C deacetylase
Reaction: cephalosporin C + H2O = deacetylcephalosporin C + acetate
For diagram of cephalosporin biosynthesis, click here
Other name(s): cephalosporin C acetyl-hydrolase; cephalosporin C acetylase; cephalosporin acetylesterase; cephalosporin C acetylesterase; cephalosporin C acetyl-esterase; cephalosporin C deacetylase
Systematic name: cephalosporin-C acetylhydrolase
Comments: Hydrolyses the acetyl ester bond on the 10-position of the antibiotic cephalosporin C.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52227-71-1
References:
1.  Fujisawa, Y., Shirafuji, H., Kida, M. and Nara, K. New findings on cephalosporin C biosynthesis. Nat. New Biol. 246 (1973) 154–155. [PMID: 4519146]
[EC 3.1.1.41 created 1976]
 
 
EC 3.5.1.93     
Accepted name: glutaryl-7-aminocephalosporanic-acid acylase
Reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate
For diagram of cephalosporin biosynthesis, click here
Other name(s): 7β-(4-carboxybutanamido)cephalosporanic acid acylase; cephalosporin C acylase; glutaryl-7-ACA acylase; CA; GCA; GA; cephalosporin acylase; glutaryl-7-aminocephalosporanic acid acylase; GL-7-ACA acylase
Systematic name: (7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase
Comments: Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56645-46-6
References:
1.  Ishii, Y., Saito, Y., Fujimura, T., Sasaki, H., Noguchi, Y., Yamada, H., Niwa, M. and Shimomura, K. High-level production, chemical modification and site-directed mutagenesis of a cephalosporin C acylase from Pseudomonas strain N176. Eur. J. Biochem. 230 (1995) 773–778. [DOI] [PMID: 7607251]
2.  Kinoshita, T., Tada, T., Saito, Y., Ishii, Y., Sato, A. and Murata, M. Crystallization and preliminary X-ray analysis of cephalosporin C acylase from Pseudomonas sp. strain N176. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 458–459. [PMID: 10739919]
3.  Monti, D., Carrea, G., Riva, S., Baldaro, E. and Frare, G. Characterization of an industrial biocatalyst: immobilized glutaryl-7-ACA acylase. Biotechnol. Bioeng. 70 (2000) 239–244. [PMID: 10972935]
4.  Kwon, T.H., Rhee, S., Lee, Y.S., Park, S.S. and Kim, K.H. Crystallization and preliminary X-Ray diffraction analysis of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp. GK16. J. Struct. Biol. 131 (2000) 79–81. [DOI] [PMID: 10945972]
5.  Kim, Y., Yoon, K.-H., Khang, Y., Turley, S. and Hol, W.G.J. The 2.0 Å crystal structure of cephalosporin acylase. Structure 8 (2000) 1059–1068. [DOI] [PMID: 11080627]
6.  Huang, X., Zeng, R., Ding, X., Mao, X., Ding, Y., Rao, Z., Xie, Y., Jiang, W. and Zhao, G. Affinity alkylation of the Trp-B4 residue of the β-subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130. J. Biol. Chem. 277 (2002) 10256–10264. [DOI] [PMID: 11782466]
7.  Kim, J.K., Yang, I.S., Rhee, S., Dauter, Z., Lee, Y.S., Park, S.S. and Kim, K.H. Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation. Biochemistry 42 (2003) 4084–4093. [DOI] [PMID: 12680762]
[EC 3.5.1.93 created 2005]
 
 
EC 5.1.1.17     
Accepted name: isopenicillin-N epimerase
Reaction: isopenicillin N = penicillin N
For diagram of penicillin-N and deacetoxycephalosporin-C biosynthesis, click here
Systematic name: penicillin-N 5-amino-5-carboxypentanoyl-epimerase
Comments: This enzyme contains pyridoxal phosphate. Epimerization at C-5 of the 5-amino-5-carboxypentanoyl group to form penicillin N is required to make a substrate for EC 1.14.20.1, deactoxycephalosporin-C synthase, to produce cephalosporins. Forms part of the penicillin biosynthesis pathway (for pathway, click here).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 88201-43-8
References:
1.  Usui, S. and Yu, C.-A. Purification and properties of isopenicillin-N epimerase from Streptomyces clavuligerus. Biochim. Biophys. Acta 999 (1989) 78–85. [DOI] [PMID: 2804141]
2.  Laiz, L., Liras, P., Castro, J.M. and Martín, J.F. Purification and characterization of the isopenicillin-N epimerase from Nocardia lactamdurans. J. Gen. Microbiol. 136 (1990) 663–671.
3.  Cantwell, C., Beckmann, R., Whiteman, P., Queener, S.W. and Abraham, E.P. Isolation of deacetoxycephalosporin-c from fermentation broths of Penicillium chrysogenum transformants - construction of a new fungal biosynthetic-pathway. Proc. R. Soc. Lond. B Biol. Sci. 248 (1992) 283–289. [DOI] [PMID: 1354366]
4.  Yeh, W.K., Ghag, S.K. and Queener, S.W. Enzymes for epimerization of isopenicillin N, ring expansion of penicillin N, and 3′-hydroxylation of deacetoxycephalosporin C. Function, evolution, refolding, and enzyme engineering. Ann. N.Y. Acad. Sci. 672 (1992) 396–408.
[EC 5.1.1.17 created 2002]
 
 


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