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Information on EC 2.3.1.226 - carboxymethylproline synthase
for references in articles please use BRENDA:EC2.3.1.226
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.226 carboxymethylproline synthase
IUBMB Comments
The enzyme is involved in the biosynthesis of the carbapenem β-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum.
The enzyme appears in viruses and cellular organisms
- 2.3.1.226
- crotonase
-
functionalised
- methylmalonyl-coa
-
carbapenams
- beta-lactams
- synthesis
- carboxylase
-
biocatalysis
-
cyclization
- synthases
-
bicyclic
-
malonyl-coenzyme
- acetyl-coa
- crotonyl-coa
-
simplest
-
stereoselective
- medicine
Reaction Schemes
showSynonyms
carboxymethylproline synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CarB
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-5-carboxymethylproline + CO2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
(5R)-carbapenem carboxylate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:(S)-1-pyrroline-5-carboxylate malonyltransferase (cyclizing)
The enzyme is involved in the biosynthesis of the carbapenem beta-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ethylmalonyl-CoA + (2S,5S)-carboxymethylproline + CO2
CoA + (2S,5S,6R)-6-ethyl-5-carboxymethylproline
-
Substrates: the substrate is an equilibrium mixture of L-glutamate semialdehyde, 5-hydroxy-L-proline and L-pyrroline-5-carboxylate. Some of the CarB variants catalyse the production of the two C6 epimers of (2S,5S)-6-ethyl-5-carboxymethylproline
Products: wild-type enzyme produces a 65:35 mixture of (6R)- and (6S)-epimer
Products: wild-type enzyme produces a 65:35 mixture of (6R)- and (6S)-epimer
?
ethylmalonyl-CoA + (2S,5S)-carboxymethylproline + CO2
CoA + (2S,5S,6S)-6-ethyl-5-carboxymethylproline
-
Substrates: the substrate is an equilibrium mixture of L-glutamate semialdehyde, 5-hydroxy-L-proline and L-pyrroline-5-carboxylate. Some of the CarB variants catalyse the production of the two C6 epimers of (2S,5S)-6-ethyl-5-carboxymethylproline
Products: wild-type enzyme produces a 65:35 mixture of (6R)- and (6S)-epimer
Products: wild-type enzyme produces a 65:35 mixture of (6R)- and (6S)-epimer
?
ethylmalonyl-CoA + L-2-aminoadipate semialdehyde
CoA + (2S,6S,7R)-7-ethyl-carboxymethylpipecolic acid
-
Substrates: activity with mutant enzymes W79F, W79F/M108A and W79F/M108V. mutant W79A: epimeric ethylmalonylĀCoA produces solely (2S,6S,7S)-(2S,6S)-carboxymethylpipecolic acid via reaction of (2R)-ethylmalonyl-CoA, whereas incubation of (2S)-ethylmalonylĀCoA and L-2-aminoadipate semialdehyde results in no detectable production of 7-ethyl-(2S,6S)-carboxymethylpipecolic acid
Products: -
Products: -
?
ethylmalonyl-CoA + L-2-aminoadipate semialdehyde
CoA + (2S,6S,7S)-7-ethyl-carboxymethylpipecolic acid
-
Substrates: activity with mutant enzymes W79F, W79F/M108A and W79F/M108V. mutant W79A: epimeric ethylmalonylĀCoA produces solely (2S,6S,7S)-(2S,6S)-carboxymethylpipecolic acid via reaction of (2R)-ethylmalonyl-CoA, whereas incubation of (2S)-ethylmalonylĀCoA and L-2-aminoadipate semialdehyde results in no detectable production of 7-ethyl-(2S,6S)-carboxymethylpipecolic acid
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-carboxymethylproline + CO2
malonyl-CoA + L-2-aminopimelate semialdehyde
CoA + (2S,7S)-7-(carboxymethyl)-azepane-2-carboxylic acid + CO2
-
Substrates: the CarB His229Ala variant is able to form the target compound in a yield of about 3 times higher than that obtained with wild-type CarB
Products: -
Products: -
?
methylmalonyl-CoA + (2S,5S)-5-carboxymethylproline + CO2
CoA + (2S,5S,6R)-6-methyl-5-carboxymethylproline
-
Substrates: the substrate is an equilibrium mixture of L-glutamate semialdehyde, 5-hydroxy-L-proline and L-pyrroline-5-carboxylate
Products: wild-type enzyme produces a 55:45 mixture of (6R)- and (6S)-epimer
Products: wild-type enzyme produces a 55:45 mixture of (6R)- and (6S)-epimer
?
methylmalonyl-CoA + (2S,5S)-5-carboxymethylproline + CO2
CoA + (2S,5S,6S)-6-methyl-5-carboxymethylproline
-
Substrates: the substrate is an equilibrium mixture of L-glutamate semialdehyde, 5-hydroxy-L-proline and L-pyrroline-5-carboxylate
Products: wild-type enzyme produces a 55:45 mixture of (6R)- and (6S)-epimer
Products: wild-type enzyme produces a 55:45 mixture of (6R)- and (6S)-epimer
?
methylmalonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-6-methyl-5-carboxymethylproline + CO2
-
Substrates: -
Products: -
Products: -
?
methylmalonyl-CoA + L-2-aminoadipate semialdehyde
CoA + (2S,6S,7R)-7-methyl-carboxymethylpipecolic acid
-
Substrates: -
Products: wild-type enzyme produces a 66:34 mixture of (7R)- and (7S)-epimer
Products: wild-type enzyme produces a 66:34 mixture of (7R)- and (7S)-epimer
?
methylmalonyl-CoA + L-2-aminoadipate semialdehyde
CoA + (2S,6S,7S)-7-methyl-carboxymethylpipecolic acid
-
Substrates: -
Products: wild-type enzyme produces a 66:34 mixture of (7R)- and (7S)-epimer
Products: wild-type enzyme produces a 66:34 mixture of (7R)- and (7S)-epimer
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
Substrates: -
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: the enzyme catalyzes committed step in the biosynthesis of (5R)-carbapenem-3-carboxylic acid, the simplest of the medicinally important carbapenem antibiotics
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: acetyl-CoA is not a substrate
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: CarB is a member of the crotonase superfamily of enzymes. In addition to decarboxylation and thioester hydrolysis steps, it catalyzes C-C bond formation leading to a substituted heterocycle. Mechanistic studies show that C-C bond formation by CarB most probably occurs by reaction of P5C with an oxy-anion stabilized enolate, and thioester hydrolysis most probably proceeds by direct attack of an activated water molecule
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: the substrate is an equilibrium mixture of L-glutamate semialdehyde, 5-hydroxy-L-proline and L-pyrroline-5-carboxylate
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-carboxymethylproline + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-carboxymethylproline + CO2
-
Substrates: the enzyme is involved in the biosynthesis of 1-carbapen-2-em-3-carboxylic acid, a simple beta-lactam antibiotic
Products: -
Products: -
?
malonyl-CoA + L-glutamate-gamma-semialdehyde
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + L-glutamate-gamma-semialdehyde
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: L-glutamate-gamma-semialdehyde but not D-glutamate-gamma-semialdehyde is a substrate of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: CarB catalyzes the independent decarboxylation of malonyl-CoA and methylmalonyl-CoA and the hydrolysis of CoA esters such as acetyl-CoA and propionyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with L-2-aminosuberate semialdehyde (wild-type enzyme and mutant enzyme H229A)
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-carboxymethylproline + CO2
malonyl-CoA + L-glutamate-gamma-semialdehyde
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
Substrates: -
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: the enzyme catalyzes committed step in the biosynthesis of (5R)-carbapenem-3-carboxylic acid, the simplest of the medicinally important carbapenem antibiotics
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-5-carboxymethylproline + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-carboxymethylproline + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O
CoA + (2S,5S)-carboxymethylproline + CO2
-
Substrates: the enzyme is involved in the biosynthesis of 1-carbapen-2-em-3-carboxylic acid, a simple beta-lactam antibiotic
Products: -
Products: -
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is involved in the carbapenem biosynthesis
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CARB_PECCC
250
0
27575
Swiss-Prot
-
A0A7W8TC87_9BURK
264
0
29089
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27575
-
3 * 27575, calculated from sequence, negative ion electrospray MS, enzyme exists predominantly in a trimeric form
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
-
3 * 27575, calculated from sequence, negative ion electrospray MS, enzyme exists predominantly in a trimeric form
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of CarB in the presence and absence of acetyl-CoA at 2.24 A and 3.15 A resolution. The structures reveal that CarB contains a conserved oxy-anion hole probably required for decarboxylation of malonyl-CoA and stabilization of the resultant enolate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H229A
M108A
-
forms the C6 epimers (6R):(6S) of (2S,5S)-6-methyl-5-carboxymethylproline in the ratio of 45:55 compared to wild-type ratio of 55:45
M108I
-
forms the C6 epimers (6R):(6S) of (2S,5S)-6-methyl-5-carboxymethylproline in the ratio of 92:8 compared to wild-type ratio of 55:45
M108L
-
forms the C6 epimers (6R):(6S) of (2S,5S)-6-methyl-5-carboxymethylproline in the ratio of 47:53 compared to wild-type ratio of 55:45. Forms the C6 epimers (6R):(6S) of (2S,5S)-6-ethyl-5-carboxymethylproline in the ratio of 72:18 compared to wild-type ratio of 65:35. Forms the C7 epimers (7R):(7S) of 7-methyl-(2S,6S)-carboxymethylpipecolic acid in the ratio of 60:40 compared to the wild-type ration of 66:34
M108V
Q111N
-
forms the C6 epimers (6R):(6S) of (2S,5S)-6-methyl-5-carboxymethylproline in the ratio of 70:30 compared to wild-type ratio of 55:45
W79A
-
forms the C6 epimers (6R):(6S) of (2S,5S)-6-methyl-5-carboxymethylproline in the ratio of 16:84 compared to wild-type ratio of 55:45. Forms the C6 epimers (6R):(6S) of (2S,5S)-6-ethyl-5-carboxymethylproline in the ratio of 12:88 compared to wild-type ratio of 65:35. Forms the C7 epimers (7R):(7S) of 7-methyl-(2S,6S)-carboxymethylpipecolic acid in the ratio of 1:99 compared to the wild-type ration of 66:34
W79F
W79F/M108A
-
forms the C6 epimers (6R):(6S) of (2S,5S)-6-methyl-5-carboxymethylproline in the ratio of 11:89 compared to wild-type ratio of 55:45. Forms the C6 epimers (6R):(6S) of (2S,5S)-6-ethyl-5-carboxymethylproline in the ratio of 17:83 compared to wild-type ratio of 65:35. Forms the C7 epimers (7R):(7S) of 7-methyl-(2S,6S)-carboxymethylpipecolic acid in the ratio of 5:95 compared to the wild-type ration of 66:34
W79F/M108V
-
forms the C6 epimers (6R):(6S) of (2S,5S)-6-methyl-5-carboxymethylproline in the ratio of 56:44 compared to wild-type ratio of 55:45. Forms the C6 epimers (6R):(6S) of (2S,5S)-6-ethyl-5-carboxymethylproline in the ratio of 34:66 compared to wild-type ratio of 65:35. Forms the C7 epimers (7R):(7S) of 7-methyl-(2S,6S)-carboxymethylpipecolic acid in the ratio of 24:76 compared to the wild-type ration of 66:34
H229A
-
forms the C6 epimers (6R):(6S) of (2S,5S)-6-methyl-5-carboxymethylproline in the ratio of 75:25 compared to wild-type ratio of 55:45
H229A
-
the CarB variant is able to form (2S,7S)-7-(carboxymethyl)-azepane-2-carboxylic acid from malonyl-CoA and L-aminopimelate semialdehyde in a yield of about 3 times higher than that obtained with wild-type CarB
M108V
-
forms the C6 epimers (6R):(6S) of (2S,5S)-6-methyl-5-carboxymethylproline in the ratio of 95:5 compared to wild-type ratio of 55:45
M108V
mutant is able to convert (2S)-methylmalonyl-CoA/L-glutamate semialdehyde/5-hydroxyproline/pyrroline-5-carboxylate to (6R)-6-methyl-(2S,5S)-5-carboxymethylproline
W79F
-
forms the C6 epimers (6R):(6S) of (2S,5S)-6-methyl-5-carboxymethylproline in the ratio of 17:83 compared to wild-type ratio of 55:45. Forms the C6 epimers (6R):(6S) of (2S,5S)-6-ethyl-5-carboxymethylproline in the ratio of 32:68 compared to wild-type ratio of 65:35. Forms the C7 epimers (7R):(7S) of 7-methyl-(2S,6S)-carboxymethylpipecolic acid in the ratio of : compared to the wild-type ration of 17:83
W79F
mutant is able to convert (2S)-ethylmalonyl-CoA/L-glutamate semialdehyde/5-hydroxyproline/pyrroline-5-carboxylate to (6R)-6-ethyl-(2S,5S)-5-carboxymethylproline
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
carboxymethylproline synthases is a biocatalysts for preparing functionalised N-heterocycles in a diastereoselective fashion. The products can be converted into the respective bicyclic beta-lactams of potential application in the semisynthesis of stable beta-lactam antibiotics
synthesis
synthesis
-
carboxymethylproline synthases is a biocatalysts for preparing functionalised N-heterocycles in a diastereoselective fashion. The products can be converted into the respective bicyclic beta-lactams of potential application in the semisynthesis of stable beta-lactam antibiotics
synthesis
coupling of methylmalonyl-CoA epimerase, crotonyl-CoA carboxylase reductase and carboxymethylproline synthase mutants in a three-enzyme one-pot sequential synthesis of functionalised C-5 carboxyalkylprolines starting from crotonyl-CoA and carbon dioxide
synthesis
biocatalytic production of bicyclic beta-lactams with three contiguous chiral centres using engineered crotonases. Structurally guided substitutions of wild type carboxymethylproline synthases enable tuning of their C-N and C-C bond forming capacity to produce 5-carboxymethylproline derivatives substituted at C-4 and C-6, from amino acid aldehyde and malonyl-CoA derivatives. Use of tandem enzyme incubations comprising an engineered carboxymethylproline synthase and an alkylmalonyl-CoA forming enzyme (i.e. malonyl-CoA synthetase or crotonyl-CoA carboxylase reductase) can improve stereocontrol and expand the product range. Some of the prepared 4,6-disubstituted-5-carboxymethylproline derivatives are converted to bicyclic beta-lactams by carbapenam synthetase catalysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Batchelar, E.T.; Hamed, R.B.; Ducho, C.; Claridge, T.D.; Edelmann, M.J.; Kessler, B.; Schofield, C.J.
Thioester hydrolysis and C-C bond formation by carboxymethylproline synthase from the crotonase superfamily
Angew. Chem. Int. Ed. Engl.
47
9322-93225
2008
Pectobacterium carotovorum
brenda
Gerratana, B.; Arnett, S.O.; Stapon, A.; Townsend, C.A.
Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase superfamily
Biochemistry
43
15936-15945
2004
Pectobacterium carotovorum
brenda
Hamed, R.B.; Mecinovic, J.; Ducho, C.; Claridge, T.D.; Schofield. C.J.
Carboxymethylproline synthase catalysed syntheses of functionalised N-heterocycles
Chem. Commun. (Camb. )
46
1413-1415
2010
Pectobacterium carotovorum
brenda
Sorensen, J.L.; Sleeman, M.C.; Schofield, C.J.
Synthesis of deuterium labelled L- and D-glutamate semialdehydes and their evaluation as substrates for carboxymethylproline synthase (CarB) - implications for carbapenem biosynthesis
Chem. Commun. (Camb. )
7
1155-1157
2005
Pectobacterium carotovorum
brenda
Sleeman, M.C.; Schofield, C.J.
Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis
J. Biol. Chem.
279
6730-6736
2004
Pectobacterium carotovorum
brenda
Sleeman, M.C.; Sorensen, J.L.; Batchelar, E.T.; McDonough, M.A.; Schofield, C.J.
Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis
J. Biol. Chem.
280
34956-34965
2005
Pectobacterium carotovorum (Q9XB60)
brenda
McGowan, S.J.; Sebaihia, M.; Porter, L.E.; Stewart, G.S.; Williams, P.; Bycroft, B.W.; Salmond, G.P.
Analysis of bacterial carbapenem antibiotic production genes reveals a novel beta-lactam biosynthesis pathway
Mol. Microbiol.
22
415-426
1996
Pectobacterium carotovorum, Pectobacterium carotovorum GS101
brenda
Hamed, R.B.; Gomez-Castellanos, J.R.; Thalhammer, A.; Harding, D.; Ducho, C.; Claridge, T.D.; Schofield. C.J.
Stereoselective C-C bond formation catalysed by engineered carboxymethylproline synthases
Nat. Chem.
3
365-371
2011
Pectobacterium carotovorum
brenda
Hamed, R.B.; Gomez-Castellanos, J.R.; Froese, D.S.; Krysztofinska, E.; Yue, W.W.; Schofield, C.J.
Use of methylmalonyl-CoA epimerase in enhancing crotonase stereoselectivity
ChemBioChem
17
1-7
2015
Pectobacterium carotovorum (Q9XB60)
brenda
Hamed, R.B.; Gomez-Castellanos, J.R.; Henry, L.; Warhaut, S.; Claridge, T.D.W.; Schofield, C.J.
Biocatalytic production of bicyclic ?-lactams with three contiguous chiral centres using engineered crotonases
Commun. Chem.
2
7
2019
Pectobacterium carotovorum subsp. carotovorum (Q9XB60)
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.1.226)
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Release 2023.1 (January 2023)
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