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1.14.11.26: deacetoxycephalosporin-C hydroxylase

This is an abbreviated version!
For detailed information about deacetoxycephalosporin-C hydroxylase, go to the full flat file.

Word Map on EC 1.14.11.26

Reaction

deacetoxycephalosporin C
+
2-oxoglutarate
 +
O2
=
deacetylcephalosporin C
 +
succinate
 +
CO2

Synonyms

cefF, Cephalosporin biosynthesis expandase/hydroxylase, DACS, DAOC hydroxylase, DAOC synthase, DAOC/DAC synthase, DAOCS, deacetoxycephalosporin C hydroxylase, deacetoxycephalosporin C synthase, deacetylcephalosporin C synthase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.26 deacetoxycephalosporin-C hydroxylase

Engineering

Engineering on EC 1.14.11.26 - deacetoxycephalosporin-C hydroxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M306I
-
hydroxylation reaction of deacetoxycephalosporin C, EC 1.14.11.26, is abolished, 59% of wild-type ring expansion activity
N305L
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
A311V
random mutagenesis
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
E16G/T90A/T304A
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
M229V
random mutagenesis
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
T273A
random mutagenesis
T90A
random mutagenesis
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
V150A
random mutagenesis
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
V221A
random mutagenesis
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
Y38C
random mutagenesis
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
-
additional information