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3'-methylcephem + 2-oxoglutarate + O2
3'-hydroxymethylcephem + succinate + CO2
-
-
-
-
?
3-exo-methylenecephalosporin C + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2
-
37% of activity with deacetoxycephalosporin C
-
-
?
3-exomethylenecephalosporin + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
3-exomethylenecephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
7-aminodeacetoxycephalosporanic acid + 2-oxoglutarate + O2
7-aminodeacetylcephalosporin + succinate + CO2
ampicillin + 2-oxoglutarate + O2
? + succinate + CO2
-
-
-
-
?
cephalexin + 2-oxoglutarate + O2
? + succinate + CO2
-
-
-
-
?
cephalosporin G + 2-oxoglutarate + O2
deacetylcephalosporin G + succinate + CO2
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin G + 2-oxoglutarate + O2
? + succinate + CO2
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
? + succinate + CO2
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
succinate + CO2 + ?
-
-
-
-
?
phenylacetyl-7-aminodeacetoxycephalosporanic acid + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetylcephalosporin + succinate + CO2
7-aminodeacetoxycephalosporanic acid + 2-oxoglutarate + O2
7-aminodeacetylcephalosporin + succinate + CO2
-
-
-
-
?
7-aminodeacetoxycephalosporanic acid + 2-oxoglutarate + O2
7-aminodeacetylcephalosporin + succinate + CO2
-
poor substrate
-
-
?
cephalosporin G + 2-oxoglutarate + O2
deacetylcephalosporin G + succinate + CO2
the wild-type enzyme shows negligible activity toward cephalosporin G, an unnatural and less expensive substrate analogue, but diverse enzyme mutants show increased to high activity with cephalosporin G, overview
-
-
?
cephalosporin G + 2-oxoglutarate + O2
deacetylcephalosporin G + succinate + CO2
the wild-type enzyme shows negligible activity toward cephalosporin G, an unnatural and less expensive substrate analogue, but diverse enzyme mutants show increased to high activity with cephalosporin G, overview
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
-
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
hydroxylation at C-3' by deacetylcephalosporin C hydroxylase
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
-
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
-
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
-
-
?
phenylacetyl-7-aminodeacetoxycephalosporanic acid + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetylcephalosporin + succinate + CO2
-
-
-
-
?
phenylacetyl-7-aminodeacetoxycephalosporanic acid + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetylcephalosporin + succinate + CO2
-
-
-
-
?
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(2S,4S,6R,7R)-1-aza-7-((5R)-5-carboxypentanamidol)-4-methyl-8-oxo-5-thiatricyclo-(4,2,0,0)octane-2-carboxylate
-
reversible, 0.04 mM, 90% inhibition
5,5'-dithiobis-2-nitrobenzoic acid
ammonium hydrogencarbonate
-
100-500 mM, complete inactivation
Co2+
-
inhibition in decreasing order, Zn2+, Co2+, Ni2+
Ni2+
-
inhibition in decreasing order, Zn2+, Co2+, Ni2+
Penicillin N
-
1 mM, 62% inhibition, competitive with deacetoxycephalosporin C
5,5'-dithiobis-2-nitrobenzoic acid
-
1 mM, 100% inhibition of hydroxylation reaction, EC 1.14.11.26
5,5'-dithiobis-2-nitrobenzoic acid
-
reactivation by dithiothreitol
5,5'-dithiobis-2-nitrobenzoic acid
-
1 mM, no residual activity
EDTA
-
0.6 mM, 83% inhibition of hydroxylation reaction, EC 1.14.11.26
EDTA
-
0.5 mM, no residual activity
iodoacetic acid
-
1 mM, 2% inhibition of hydroxylation reaction, EC 1.14.11.26
iodoacetic acid
-
1 mM, 19% residual activity
N-ethylmaleimide
-
-
N-ethylmaleimide
-
1 mM, 97% inhibition of hydroxylation reaction, EC 1.14.11.26
N-ethylmaleimide
-
1 mM, no residual activity
o-phenanthroline
-
0.6 mM, 100% inhibition of hydroxylation reaction, EC 1.14.11.26
o-phenanthroline
-
0.5 mM, no residual activity
p-hydroxymercuribenzoate
-
1 mM, 100% inhibition of hydroxylation reaction, EC 1.14.11.26
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
0.1 mM, no residual activity
Zn2+
-
strong
Zn2+
-
inhibition in decreasing order, Zn2+, Co2+, Ni2+
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evolution
the enzyme belongs to the family of 2-oxoglutarate-dependent oxygenases
evolution
-
the enzyme belongs to the family of 2-oxoglutarate-dependent oxygenases
-
metabolism
the enzyme from Acremonium chrysogenum is bifunctional and catalyzes both the synthesis of deacetoxycephalosporin C from penicillin N, EC 1.14.20.1, as well as the hydroxylation of deacetoxycephalosporin C to deacetylcephalosporin C, EC 1.14.11.26. The activities are located on two different domains
metabolism
two enzymes, deacetoxycephalosporin C synthase and deacetoxycephalosporin C hydroxylase, are involved in the conversion of penicillin N into deacetylcephalosporin C in Streptomyces clavuligerus
metabolism
deacetylcephalosporin C synthase (DACS) transforms an inert methyl group of deacetoxycephalosporin C (DAOC) into an active hydroxyl group of deacetylcephalosporin C (DAC) during the biosynthesis of cephalosporins
metabolism
-
the enzyme from Acremonium chrysogenum is bifunctional and catalyzes both the synthesis of deacetoxycephalosporin C from penicillin N, EC 1.14.20.1, as well as the hydroxylation of deacetoxycephalosporin C to deacetylcephalosporin C, EC 1.14.11.26. The activities are located on two different domains
-
metabolism
-
deacetylcephalosporin C synthase (DACS) transforms an inert methyl group of deacetoxycephalosporin C (DAOC) into an active hydroxyl group of deacetylcephalosporin C (DAC) during the biosynthesis of cephalosporins
-
metabolism
-
two enzymes, deacetoxycephalosporin C synthase and deacetoxycephalosporin C hydroxylase, are involved in the conversion of penicillin N into deacetylcephalosporin C in Streptomyces clavuligerus
-
physiological function
the enzyme is involved in the biosynthesis of cephalosporins, it carries out a critical transformation of an inert cephem methyl group of deacetoxycephalosporin C (DAOC) into an active hydroxyl group of deacetylcephalosporin C (DAC) in the presence of iron, oxygen, ascorbic acid, and 2-oxoglutarate. It is a step which is chemically difficult to accomplish and which offers a second substitution site for derivatization in cephalosporins
physiological function
-
the enzyme is involved in the biosynthesis of cephalosporins, it carries out a critical transformation of an inert cephem methyl group of deacetoxycephalosporin C (DAOC) into an active hydroxyl group of deacetylcephalosporin C (DAC) in the presence of iron, oxygen, ascorbic acid, and 2-oxoglutarate. It is a step which is chemically difficult to accomplish and which offers a second substitution site for derivatization in cephalosporins
-
additional information
additional recombinant expression of gene cefF from Streptomyces clavuligerus in Acremonium chrysogenum strain CGMCC3.3795 leads to a reduction of the content of deacetoxycephalosporin C in the cephalosporin C fermentation broth, quantitative PCR expression analysis, overview
additional information
-
additional recombinant expression of gene cefF from Streptomyces clavuligerus in Acremonium chrysogenum strain CGMCC3.3795 leads to a reduction of the content of deacetoxycephalosporin C in the cephalosporin C fermentation broth, quantitative PCR expression analysis, overview
additional information
homology modeling of DACS structure
additional information
-
homology modeling of DACS structure
additional information
-
additional recombinant expression of gene cefF from Streptomyces clavuligerus in Acremonium chrysogenum strain CGMCC3.3795 leads to a reduction of the content of deacetoxycephalosporin C in the cephalosporin C fermentation broth, quantitative PCR expression analysis, overview
-
additional information
-
homology modeling of DACS structure
-
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M306I
-
hydroxylation reaction of deacetoxycephalosporin C, EC 1.14.11.26, is abolished, 59% of wild-type ring expansion activity
R308L
-
improved ability to convert penicillin analogs in ring expansion reaction of EC 1.14.20.1
W82S
-
44% of wild-type ring expansion activity, 18% of wild-type hydroxylation activity
A106T
-
80% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
A177V
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
C155Y
-
90% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
C155Y/Y184H/V275I/C281Y
-
580% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
C281Y
-
200% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
E209Q
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
E82D
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
F267L
random mutagenesis, active site mutation, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
G300V
-
410% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
G79E
-
90% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
H244Q
-
140% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
I193V
random mutagenesis, active site mutation, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
I305L
-
230% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
I305M
-
380% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
L236V
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
L277Q
-
270% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
M184I
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
M188I
-
90% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
M188V
-
150% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
M73T
-
180% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
N304K
-
220% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
P186L
random mutagenesis and site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
P72L
random mutagenesis and site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
R182S
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
R182W
random mutagenesis, active site mutation, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
S251F
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
S260G
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/A311V
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/M184I/I193V/F267L
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/R182S
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/S251F
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/S260G
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V171L/F267L
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V171L/R182W/F267L
site-directed mutagenesis, the mutant shows highly increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V171L/R182W/F267L/A241V/V307A
site-directed mutagenesis, the mutant shows highly increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V171L/R182W/F267L/G108D
site-directed mutagenesis, the mutant shows highly increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V171L/R182W/F267L/N313D
site-directed mutagenesis, the mutant shows highly increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V171L/R182W/F267L/R91G
site-directed mutagenesis, the mutant shows highly increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V171L/R182W/F267L/R91G/A241V/V307A
site-directed mutagenesis, the mutant shows highly increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V171L/R182W/F267L/T96S/A241V/V307A
site-directed mutagenesis, the mutant shows highly increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V171L/R182W/F267L/T96S/G255D/A280S
site-directed mutagenesis, the mutant shows highly increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V171L/R182W/F267L/V226I
site-directed mutagenesis, the mutant shows highly increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/A40V/M229I/T273A/V221P
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/F195L
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/P7L/A237V
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/P7L/T273A
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/R250L
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/V206I/A210V
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T90A/P72L/A311V/V206I/A210V/T273A
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
T91A
-
110% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
V171L
random mutagenesis, active site mutation, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
V171M
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
V221H
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
V221P
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
V221T
random mutagenesis and site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
V249I
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
V275I
-
270% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
V275I/I305M
-
500% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
Y184H
-
200% relative activity compared to the wild type enzyme using 1 mM penicillin G as substrate
A177V
-
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
-
E82D
-
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
-
T90A
-
random mutagenesis
-
V221A
-
random mutagenesis
-
N305L
-
107% of wild-type ring expansion activity, 85% of wild-type hydroxylation activity
N305L
-
improved ability to convert penicillin analogs in ring expansion reaction of EC 1.14.20.1
W82A
-
5.5% of wild-type ring expansion activity, 71% of wild-type hydroxylation activity
W82A
-
ring expansion reaction of EC 1.14.20.1 is reduced
E16G/T90A/T304A
random mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
E16G/T90A/T304A
site-directed mutagenesis, the mutant shows increased activity with cephalosporin G compared to the wild-type enzyme
additional information
-
truncation of C-terminus to residue 310, 2fold enhancement of ring expansion reaction of penicillin G. Double mutant with truncation at residue 310 and M306I, selective catalyzation of ring expansion. Triple mutant with truncation at residue 310, M306I and N305L, selective catalization of ring expansion with improved kinetic parameters
additional information
mutagenic cefF library creation by random mutagenesis and screening of the mutant deacetylcephalosporin C synthase enzyme library, homology modeling of DACS structure and mapping of mutant positions. Process-level biotransformation reaction of cephalosporin G to deacetylcephalosporin G by mutants of deacetylcephalosporin C synthase. Deacetylcephalosporin G can be converted completely into hydroxymethyl-7-amino-cephalosporanic acid (HACA) in about 30 min by a subsequent reaction, thus facilitating scalability toward commercialization. Directed-evolution strategies such as random, semirational, rational, and computational methods are used for systematic engineering of DACS for improved activity with cephalosporin G
additional information
-
mutagenic cefF library creation by random mutagenesis and screening of the mutant deacetylcephalosporin C synthase enzyme library, homology modeling of DACS structure and mapping of mutant positions. Process-level biotransformation reaction of cephalosporin G to deacetylcephalosporin G by mutants of deacetylcephalosporin C synthase. Deacetylcephalosporin G can be converted completely into hydroxymethyl-7-amino-cephalosporanic acid (HACA) in about 30 min by a subsequent reaction, thus facilitating scalability toward commercialization. Directed-evolution strategies such as random, semirational, rational, and computational methods are used for systematic engineering of DACS for improved activity with cephalosporin G
additional information
-
mutagenic cefF library creation by random mutagenesis and screening of the mutant deacetylcephalosporin C synthase enzyme library, homology modeling of DACS structure and mapping of mutant positions. Process-level biotransformation reaction of cephalosporin G to deacetylcephalosporin G by mutants of deacetylcephalosporin C synthase. Deacetylcephalosporin G can be converted completely into hydroxymethyl-7-amino-cephalosporanic acid (HACA) in about 30 min by a subsequent reaction, thus facilitating scalability toward commercialization. Directed-evolution strategies such as random, semirational, rational, and computational methods are used for systematic engineering of DACS for improved activity with cephalosporin G
-
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Ghag, S.K.; Brems, D.N.; Hassell, T.C.; Yeh, W.K.
Refolding and purification of Cephalosporium acremonium deacetoxycephalosporin C synthetase/hydroxylase from granules of recombinant Escherichia coli
Biotechnol. Appl. Biochem.
24
109-119
1996
Acremonium chrysogenum
brenda
Dotzlaf, J.E.; 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
10219-10227
1989
Streptomyces clavuligerus
brenda
Lloyd, M.D.; Lipscomb, S.J.; Hewitson, K.S.; Hensgens, C.M.H.; Baldwin, J.E.; Schofield, C.J.
Controlling the substrate selectivity of deacetoxycephalosporin/deacetylcephalosporin C synthase
J. Biol. Chem.
279
15420-15426
2004
Acremonium chrysogenum
brenda
Coque, J.J.; Enguita, F.J.; Cardoza, R.E.; Martin, J.F.; 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
605-609
1996
Amycolatopsis lactamdurans
brenda
Samson, S.M.; Dotzlaf, J.E.; Slisz, M.L.; Becker, G.W.; Van Frank, R.M.; Veal, L.E.; Yeh, W.K.; Miller, J.R.; Queener, S.W.; Ingolia, T.D.
Cloning and expression of the fungal expandase/hydroxylase gene involved in cephalosporin biosynthesis
Bio/Technology
5
1207-1214
1987
Acremonium chrysogenum
-
brenda
Baldwin, J.E.; Adlington, R.M.; Coates, J.B.; Crabbe, M.J.; Crouch, N.P.; Keeping, J.W.; Knight, G.C.; Schofield, C.J.; Ting, H.H.; Vallejo, C.A.; et al.
Purification and initial characterization of an enzyme with deacetoxycephalosporin C synthetase and hydroxylase activities
Biochem. J.
245
831-841
1987
Acremonium chrysogenum
brenda
Wu, X.B.; Fan, K.Q.; Wang, Q.H.; Yang, K.Q.
C-terminus mutations of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase with improved activity toward penicillin analogs
FEMS Microbiol. Lett.
246
103-110
2005
Acremonium chrysogenum
brenda
Jensen, S.E.; Westlake, D.W.S.; Wolfe, S.
Deacetoxycephalosporin C synthetase and deacetoxycephalosporin C hydroxylase are two separate enzymes in Streptomyces clavuligerus
J. Antibiot.
38
263-265
1985
Streptomyces clavuligerus
brenda
Dotzlaf, J.E.; Yeh, W.K.
Copurification and characterization of deacetoxycephalosporin C synthetase/hydroxylase from Cephalosporium acremonium
J. Bacteriol.
169
1611-1618
1987
Acremonium chrysogenum
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Baker, B.J.; Dotzlaf, J.E.; Yeh, W.K.
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