1.14.20.1: deacetoxycephalosporin-C synthase
This is an abbreviated version!
For detailed information about deacetoxycephalosporin-C synthase, go to the full flat file.
Word Map on EC 1.14.20.1
-
1.14.20.1
-
clavuligerus
-
chrysogenum
-
acremonium
-
isopenicillin
-
penicillium
-
beta-lactams
-
epimerase
-
cephamycins
-
cephalosporium
-
ring-expansion
-
7-aminodeacetoxycephalosporanic
-
pcbab
-
ironii
-
cephem
-
lactamdurans
-
synthesis
-
7-adca
-
2-oxoglutarate-dependent
-
cephalexin
-
carbenicillin
-
doacs
-
biotechnology
-
medicine
- 1.14.20.1
- clavuligerus
- chrysogenum
- acremonium
- isopenicillin
- penicillium
- beta-lactams
-
epimerase
-
cephamycins
- cephalosporium
-
ring-expansion
-
7-aminodeacetoxycephalosporanic
-
pcbab
-
ironii
-
cephem
- lactamdurans
- synthesis
-
7-adca
-
2-oxoglutarate-dependent
- cephalexin
- carbenicillin
-
doacs
- biotechnology
- medicine
Reaction
Synonyms
acDAOC/DACS, cefE, cefEF, Cephalosporin biosynthesis expandase/hydroxylase, DAOC synthase, DAOC/DAC synthase, DAOC/DACS, DAOCS, deacetoxy/deacetylcephalosporin C synthase, deacetoxycephalosporin C synthase, deacetoxycephalosporin-C synthase, deacetoxycephalosporin-C synthetase, deacetoxycephalosporin/deacetylcephalosporin C synthase, expandase, expendase, penicillin N expandase, scDAOCS
ECTree
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Substrates Products
Substrates Products on EC 1.14.20.1 - deacetoxycephalosporin-C synthase
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REACTION DIAGRAM
(2S,5R,6R)-3,3-dimethyl-7-oxo-6-[(thiophen-2-ylacetyl)amino]-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid + 2-oxoglutarate + O2
(6R,7R)-3-methyl-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid + succinate + CO2 + H2O
-
-
-
?
3-exomethylenecephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2 + H2O
-
8% of the activity with cephalosporin N, recombinant enzyme
-
?
7-aminodeacetoxycephalosporanic acid + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
low activity, hydroxylation reaction
-
-
ir
acetyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
7-acetylaminodesacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
adipyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
7-adipylaminodesacetoxycephalosporanic acid + succinate + CO2 + H2O
ampicillin + 2-oxo-4-methyl-pentanoic acid + O2
?
mutants R258H, R258K, R258Q, R258A, R258L, R258F, no activity with the wild-type enzyme
-
-
ir
ampicillin + 2-oxo-4-methylpentanoate + O2
cephalexin + succinate + CO2 + H2O
wild-type enzyme has a requirement for 2-oxoglutarate and cannot efficiently use hydrophobic 2-oxoacids, the mutants R258A, R258L, R258H and R258F have broadened cosubstrate selectivity and are able to utilize hydrophobic 2-oxoacids
-
?
ampicillin + 2-oxohexanoate + O2
cephalexin + ?
wild-type enzyme has a requirement for 2-oxoglutarate and cannot efficiently use hydrophobic 2-oxoacids, the mutants R258A, R258L, R258H and R258F have broadened cosubstrate selectivity and are able to utilize hydrophobic 2-oxoacids
-
-
?
ampicillin + 2-oxohexanoic acid + O2
?
mutants R258H, R258K, R258Q, R258A, R258L, R258F, no activity with the wild-type enzyme
-
-
ir
butyryl-6-aminopenicillanic acid + 2-oxoglutarate + O2
7-butyrylaminocephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
cephalexin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
low activity, hydroxylation reaction
-
-
ir
D-carboxymethylcysteinyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
?
-
-
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
decanoyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
7-decanoylaminodesacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
heptanoyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
7-heptanoylaminodesacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
hexanoyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
7-hexanoylaminodesacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
N-((thiophen-2-yl)acetyl)-6-aminopenicillanic acid + 2-oxoglutarate + O2
N-[(5R,6R)-3,3-dimethyl-2,7-dioxo-4-thia-1-azabicyclo[3.2.0]hept-6-yl]-2-(thiophen-2-yl)acetamide + succinate + CO2 + H2O
-
-
-
?
N-acetyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N-acetyldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-adipyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N-adipyldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-adipyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N7-adipylaminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
N-butyryl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N-butyryldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-decanoyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N-decanoyldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-heptanoyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N-heptanoyldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-hexanoyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N-hexanoyldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-nonanoyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N-nonanoyldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-nonanoyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N7-nonanoyldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-octanoyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N-octanoyldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-octanoyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N7-octanoyldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-valeryl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N-valeryldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
N-valeryl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N7-pentanoyldeacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin F + 2-oxoglutarate + O2
7-((3E)-hex-3-enoyl)aminocephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
penicillin G + 2-oxo-4-methyl-pentanoic acid + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + 3-methylbutanoate + CO2 + H2O
mutants R258H, R258K, R258Q, R258A, R258L, R258F, no activity with the wild-type enzyme
-
-
ir
penicillin G + 2-oxo-4-methylpentanoate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + ?
penicillin G + 2-oxoglutarate + O2
7-phenylacetylaminocephalosporanate + succinate + CO2 + H2O
penicillin G + 2-oxoglutarate + O2
7-phenylacetylaminocephalosporanic acid + succinate + CO2 + H2O
low catalytic effciency towards penicillin G
-
-
?
penicillin G + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + succinate + CO2 + H2O
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
penicillin G + 2-oxohexanoic acid + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + pentanoate + CO2 + H2O
mutants R258H, R258K, R258Q, R258A, R258L, R258F, no activity with the wild-type enzyme
-
-
ir
penicillin mX + 2-oxoglutarate + O2
7-[(3-hydroxyphenyl)acetyl]aminocephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
penicillin X + 2-oxoglutarate + O2
7-[(4-hydroxyphenyl)acetyl]aminocephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
phenyl-7-aminodeacetoxycephalosporanic acid + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
hydroxylation reaction
-
-
ir
? + succinate + CO2 + H2O
-
-
-
?
6-alpha-methylpenicillin N + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
best substrate in the ring expansion reaction
-
-
ir
? + succinate + CO2 + H2O
-
-
-
?
6-aminopenicillanic acid + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
-
?
6-aminopenicillanic acid + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
low activity, ring expansion reaction
-
-
ir
? + succinate + CO2 + H2O
-
-
-
?
acetyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
ring expansion reaction
-
-
ir
7-adipylaminodesacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
adipyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
7-adipylaminodesacetoxycephalosporanic acid + succinate + CO2 + H2O
poor substrate
-
?
adipyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
7-adipylaminodesacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
? + succinate + CO2 + H2O
-
-
-
?
adipyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
ring expansion reaction
-
-
ir
? + succinate + CO2 + H2O
-
-
-
?
amoxicillin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
low activity, ring expansion reaction
-
-
ir
amoxicillin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
mutant R308L, 100% of activity, compared to wild-type
-
-
?
amoxicillin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
-
?
? + succinate + CO2
-
-
-
?
? + succinate + CO2 + H2O
-
-
-
?
ampicillin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
ring expansion reaction
-
-
ir
cephalexin + succinate + CO2 + H2O
-
mutant N305L, 222%, mutant R307L, 100%, mutant R308L, 311% of activity, compared to wild-type
-
-
?
ampicillin + 2-oxoglutarate + O2
cephalexin + succinate + CO2 + H2O
-
-
?
ampicillin + 2-oxoglutarate + O2
cephalexin + succinate + CO2 + H2O
-
-
-
-
?
ampicillin + 2-oxoglutarate + O2
cephalexin + succinate + CO2 + H2O
-
no activity
-
-
?
ampicillin + 2-oxoglutarate + O2
cephalexin + succinate + CO2 + H2O
-
-
-
?
? + succinate + CO2
-
-
-
?
? + succinate + CO2 + H2O
-
-
-
-
?
carbenicillin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
mutant N305L, 178%, mutant R307L, 93%, mutant R308L, 194% of activity, compared to wild-type
-
-
?
carbenicillin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
-
?
carbenicillin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
?
deacetylcephalosporin C + succinate + CO2
-
-
-
ir
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
-
-
-
ir
deacetoxycephalosporin C + 2-oxoglutarate + O2
deacetylcephalosporin C + succinate + CO2
the penicillin /cephem substrate are bound by residues R161 and R163
-
-
ir
? + succinate + CO2 + H2O
-
-
-
-
?
metampicillin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
?
N7-adipylaminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
?
N-adipyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N7-adipylaminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
?
N-adipyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N7-adipylaminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
?
N-adipyl-6-aminopenicillanic acid + 2-oxoglutarate + O2
N7-adipylaminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
?
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + ?
-
-
-
?
penicillin G + 2-oxo-4-methylpentanoate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + ?
wild-type enzyme has a requirement for 2-oxoglutarate and cannot efficiently use hydrophobic 2-oxoacids, the mutants R258A, R258L, R258H and R258F have broadened cosubstrate selectivity and are able to utilize hydrophobic 2-oxoacids
-
-
?
7-phenylacetylaminocephalosporanate + succinate + CO2 + H2O
-
-
-
?
penicillin G + 2-oxoglutarate + O2
7-phenylacetylaminocephalosporanate + succinate + CO2 + H2O
-
-
-
?
penicillin G + 2-oxoglutarate + O2
7-phenylacetylaminocephalosporanate + succinate + CO2 + H2O
-
-
-
?
penicillin G + 2-oxoglutarate + O2
7-phenylacetylaminocephalosporanate + succinate + CO2 + H2O
-
-
-
?
? + succinate + CO2
-
-
-
?
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + succinate + CO2 + H2O
-
mutant N305L, 163%, mutant R307L, 100%, mutant R308L, 516% of activity, compared to wild-type
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + succinate + CO2 + H2O
-
no activity
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + succinate + CO2 + H2O
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + succinate + CO2 + H2O
-
no activity
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
ir
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
the penicillin /cephem substrates are bound by residues R161 and R163
-
-
ir
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
ir
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
ir
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
ir
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
product is the precursor of 7-aminodeacetoxycephalosporanic acid, which is used in industrial applications
-
ir
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
-
?
penicillin G + 2-oxoglutarate + O2
phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
-
-
ir
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + ?
-
-
-
?
penicillin G + 2-oxohexanoate + O2
phenylacetyl-7-aminodeacetoxy cephalosporanic acid + ?
wild-type enzyme has a requirement for 2-oxoglutarate and cannot efficiently use hydrophobic 2-oxoacids, the mutants R258A, R258L, R258H and R258F have broadened cosubstrate selectivity and are able to utilize hydrophobic 2-oxoacids
-
-
?
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
ir
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
ir
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
almost absolute requirement for 2-oxoglutarate
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
bifunctional enzyme: penicillin N expandase/DAOC hydroxylase
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
2-oxoglutarate is required, residues M181, R259, and S261 might be responsible for binding of 2-oxoglutarate, the penicillin /cephem substrate are bound by residues R161 and R163
-
-
ir
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
ring expansion of penicillin N to a six member cephem ring, the natural enzyme is only able to use 2-oxoglutarate but not 2-oxobutyrate, 3-oxoadipate, 2-oxohexanoic acid or 2-oxo-4-methylpentanoic acid as cosubstrates
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
oxoglutarate analogs are not used as substrate
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
ir
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
ir
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
wild-type enzyme has a requirement for 2-oxoglutarate and cannot efficiently use hydrophobic 2-oxoacids, the mutants R258A, R258L, R258H and R258F have broadened cosubstrate selectivity and are able to utilize hydrophobic 2-oxoacids
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
separate genes encode penicillin N expandase and DAOC hydroxylase
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
the enzyme catalyzes the committed step in the biosynthesis of cephalosporin antibiotics
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
committed step in biosynthesis of cephamycin C
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
the enzyme is involved in catalyzing the biosynthesis of cephalosporins and cephamycin
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
first step in cephamycin C biosynthetic pathway
-
-
ir
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
key step in the cephamycin C biosynthesis pathway, the ring expansion step by incorporation of a methyl group into the cephem ring
-
-
ir
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
oxidative ring expansion via reactive iron-oxygen intermediate
-
-
ir
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
specific for 2-oxoglutarate, which cannot be substituted by other 2-oxoacids e.g. 2-oxohexanoic acid, or 2-oxo-4-methyl-pentanoic acid
-
-
ir
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
about 3%, compared to activity of EC 1.14.11.26, deacetoxycephalosporin hydroxylase
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
the enzyme catalyzes the ring expansion of penicillin substrates into a ring-expanded product to eventually produce cephamycin C
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
the enzyme catalyzes the ring expansion of penicillin substrates into a ring-expanded product to produce cephamycin C
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
DAOCS-catalyzed penicillin N ring expansion, NMR structure analysis, overview
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
ring expansion of penicillin N
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
the enzyme catalyzes the ring expansion of penicillin substrates into a ring-expanded product to eventually produce cephamycin C
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
DAOCS-catalyzed penicillin N ring expansion, NMR structure analysis, overview
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
ring expansion of penicillin N
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
?
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
-
-
-
ir
penicillin N + 2-oxoglutarate + O2
deacetoxycephalosporin C + succinate + CO2 + H2O
first step in cephamycin C biosynthetic pathway
-
-
ir
? + succinate + CO2 + H2O
-
-
-
?
penicillin V + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
-
?
penicillin V + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
low activity, ring expansion reaction
-
-
ir
penicillin V + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
mutant N305L, 100%, mutant R307L, 93%, mutant R308L, 170% of activity, compared to wild-type
-
-
?
penicillin V + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
-
?
penicillin V + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
no activity
-
-
?
? + succinate + CO2
-
-
-
?
? + succinate + CO2 + H2O
-
-
-
-
?
phenethicillin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
?
?
-
-
the enzyme catalyzes the first and second step in the cephamycin C biosynthetic pathway
-
-
?
additional information
?
-
the enzyme catalyzes the first and second step in the cephamycin C biosynthetic pathway
-
-
?
additional information
?
-
-
deacetoxycephem substrate specificity for the hydroxylation reaction, penam substrate specificity of the bifunctional enzyme for the ring-expansion reation, overview
-
-
?
additional information
?
-
deacetoxycephem substrate specificity for the hydroxylation reaction, penam substrate specificity of the bifunctional enzyme for the ring-expansion reation, overview
-
-
?
additional information
?
-
-
substrate specificity, oxacillin, penicillin V, and amoxicillin are no substrate
-
-
?
additional information
?
-
substrate specificity, oxacillin, penicillin V, and amoxicillin are no substrate
-
-
?
additional information
?
-
-
no substrate: pyruvate, 2-oxoadipate
-
-
?
additional information
?
-
-
a bifunctional enzyme that catalyzes both the ring-expansion of penicillin N to deacetoxycephalosporin C and the hydroxylation of the latter to deacetylcephalosporin C
-
-
?
additional information
?
-
-
role of residue R308 in controlling substrate selectivity, substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
no activity with isopenicillin N or 6-aminopenicillanic acid
-
-
?
additional information
?
-
-
does not use isopenicillin N or 6-aminopenicillanic acid as substrates, the natural enzyme is only able to use 2-oxoglutarate but not 2-ketobutyrate, 3-ketoadipate, 2-ketohexanoic acid, or 2-keto-4-methylpentanoic acid as cosubstrates
-
-
?
additional information
?
-
-
does not use isopenicillin N or 6-aminopenicillanic acid as substrates, the natural enzyme is only able to use 2-oxoglutarate but not 2-ketobutyrate, 3-ketoadipate, 2-ketohexanoic acid, or 2-keto-4-methylpentanoic acid as cosubstrates
-
-
?
additional information
?
-
-
substrate specificity, amoxicillin, penicillin V, and oxacillin are no substrate
-
-
?
additional information
?
-
-
has no hydroxylase activity of EC 1.14.11.26
-
-
?
additional information
?
-
-
no substrate: isopenicillin N, penicillin G, penicillin V, ampicillin, 6-aminopenicillanic acid
-
-
?
additional information
?
-
-
does not use isopenicillin N or 6-aminopenicillanic acid as substrates, the natural enzyme is only able to use 2-oxoglutarate but not 2-ketobutyrate, 3-ketoadipate, 2-ketohexanoic acid, or 2-keto-4-methylpentanoic acid as cosubstrates
-
-
?
additional information
?
-
enzyme is able to convert a wide range of penicillin substrates differing in their side chains, it is a member of 2-oxoglutarate-dependent dioxygenase protein family, the mechanism involves initial activation of the iron centre by 2-oxoglutarate binding followed by oxidative decarboxylation of 2-oxoglutarate to generate oxidizing ferryl species with succinate and carbon dioxide as by-products, succinate remains bound and stabilizes the reactive iron species until the substrate enters the active site, binding of penicillin to the reactive iron species via the sulfur group subsequently expels succinate and leads to oxidative ring expansion of the substrate
-
-
?
additional information
?
-
-
enzyme is able to convert a wide range of penicillin substrates differing in their side chains, it is a member of 2-oxoglutarate-dependent dioxygenase protein family, the mechanism involves initial activation of the iron centre by 2-oxoglutarate binding followed by oxidative decarboxylation of 2-oxoglutarate to generate oxidizing ferryl species with succinate and carbon dioxide as by-products, succinate remains bound and stabilizes the reactive iron species until the substrate enters the active site, binding of penicillin to the reactive iron species via the sulfur group subsequently expels succinate and leads to oxidative ring expansion of the substrate
-
-
?
additional information
?
-
-
Streptomyces clavuligerus deacetoxycephalosporin C synthase is an iron- and 2-ketoglutarate-dependent oxidase, with the ability to catalyze the ring expansion reaction of penicillins, which converts the thiazolidine ring in penicillins to the dihydrothiazine ring. scDAOCS converts its natural substrate, penicillin N, whereas it has very low activity on the bulk and cheap penicillins such as penicillin G
-
-
?
additional information
?
-
purified recombinant enzyme DAOCS expressed in Escherichia coli catalyzes the ring expansion of penicillin N but shows no hydroxylation activity for DAOC, EC 1.14.11.26
-
-
?
additional information
?
-
-
Streptomyces clavuligerus deacetoxycephalosporin C synthase is an iron- and 2-ketoglutarate-dependent oxidase, with the ability to catalyze the ring expansion reaction of penicillins, which converts the thiazolidine ring in penicillins to the dihydrothiazine ring. scDAOCS converts its natural substrate, penicillin N, whereas it has very low activity on the bulk and cheap penicillins such as penicillin G
-
-
?
additional information
?
-
-
does not use isopenicillin N or 6-aminopenicillanic acid as substrates, the natural enzyme is only able to use 2-oxoglutarate but not 2-ketobutyrate, 3-ketoadipate, 2-ketohexanoic acid, or 2-keto-4-methylpentanoic acid as cosubstrates
-
-
?
additional information
?
-
purified recombinant enzyme DAOCS expressed in Escherichia coli catalyzes the ring expansion of penicillin N but shows no hydroxylation activity for DAOC, EC 1.14.11.26
-
-
?
additional information
?
-
enzyme is able to convert a wide range of penicillin substrates differing in their side chains, it is a member of 2-oxoglutarate-dependent dioxygenase protein family, the mechanism involves initial activation of the iron centre by 2-oxoglutarate binding followed by oxidative decarboxylation of 2-oxoglutarate to generate oxidizing ferryl species with succinate and carbon dioxide as by-products, succinate remains bound and stabilizes the reactive iron species until the substrate enters the active site, binding of penicillin to the reactive iron species via the sulfur group subsequently expels succinate and leads to oxidative ring expansion of the substrate
-
-
?
additional information
?
-
-
substrate specificity, oxacillin is no substrate
-
-
?
additional information
?
-
substrate specificity, oxacillin is no substrate
-
-
?