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Information on EC 4.2.1.113 - o-succinylbenzoate synthase and Organism(s) Escherichia coli and UniProt Accession P29208

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.113 o-succinylbenzoate synthase
IUBMB Comments
Belongs to the enolase superfamily and requires divalent cations, preferably Mg2+ or Mn2+, for activity. Forms part of the vitamin-K-biosynthesis pathway.
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This record set is specific for:
Escherichia coli
UNIPROT: P29208
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
osbs, o-succinylbenzoate synthase, osb synthase, mtb-osbs, exiosbs, aaosbs, o-succinylbenzoic acid synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
o-succinylbenzoic acid synthase
-
-
OSB synthase
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydration
SYSTEMATIC NAME
IUBMB Comments
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate hydrolyase (2-succinylbenzoate-forming)
Belongs to the enolase superfamily and requires divalent cations, preferably Mg2+ or Mn2+, for activity. Forms part of the vitamin-K-biosynthesis pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
97089-83-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
show the reaction diagram
-
-
-
?
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
4-(2-carboxyphenyl)-4-oxobutyrate + H2O
show the reaction diagram
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
show the reaction diagram
-
-
-
?
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
4-(2-carboxyphenyl)-4-oxobutyrate + H2O
show the reaction diagram
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
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tightly bound to the enzyme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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restores activity of enzyme inactivated by EDTA
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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loses all activity during treatment with EDTA, activity is most efficiently restored by Mn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.078 - 0.304
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
0.0096 - 0.343
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4 - 80
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
0.4 - 94
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13 - 1000
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
3.8 - 2000
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
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pH 7.5: about 60% of maximal activity, pH 9.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 60
-
about 30% of maximal activity at 37°C and at 60°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
o-succinylbenzoate synthase is a member of the enolase superfamily
metabolism
o-succinylbenzoate synthase catalyzes a step in menaquinone biosynthesis
evolution
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the enzyme belongs to the o-succinylbenzoate synthase (OSBS) family, which is part of the enolase superfamily. Some enzymes in the OSBS family catalyze another reaction, N-succinylamino acid racemization (NSAR). NSARs cannot be segregated into a separate family because their sequences are highly similar to those of known OSBSs, and many of them have both OSBS and NSAR activities. Phylogenetic and sequence analysis
metabolism
-
the enzyme is required for menaquinone biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35760
mass spectrometry
37740
mass spectrometry
195500
-
gel filtration
66500
-
x * 66500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 66500, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-crystallization of the K133R mutant with 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
crystallization of the apoenzyme and a complex with Mg2+ and 4-(2-carboxyphenyl)-4-oxobutyrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G295A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
K133A
inactive mutant
K133R
inactive mutant
K133S
inactive mutant
K235A
inactive mutant
K235R
inactive mutant
K235S
inactive mutant
F51A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F51Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G16P/V17F/V18R/L19T/R20S/D21F/R22G/R23T/L24QL48A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G288A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, G288A introduces a steric clash with the substrate, reducing kcat/KM over 500fold
I265A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L109A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L19A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L48A/F51A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L48M
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L48M/F51Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R159M
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S262A/S263A/S264A/I265A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S262G
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S262T
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S263G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S264A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T291S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V233N
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
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20s loop is truncated by deleting residues V17, V18, L19, R20, D21, R22, R23, and L24 resulting in a mutant with highly reduced activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of a recombinant His-tagged enzyme by affinity chromatography followed by tag cleavage and anion-exchange chromatography
recombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BW25113 menC- by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli of several recombinant mutant enzymes
expression of a recombinant enzyme in Escherichia coli
gene menC, expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BW25113 menC-
gene menC, phylogenetic analysis, expression of wild-type enzme in Escherichia coli strain BL21(DE3), expression of mutant enzymes in Escherichia coli strain BW25113 (menC::kan), which is converted into a DE3 strain to express T7 RNA polymerase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thompson, T.B.; Garrett, J.B.; Taylor, E.A.; Meganathan, R.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate
Biochemistry
39
10662-10676
2000
Escherichia coli (P29208), Escherichia coli
Manually annotated by BRENDA team
Klenchin, V.A.; Taylor Ringia, E.A.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activity in the enolase superfamily: structural and mutagenic studies of the mechanism of the reaction catalyzed by o-succinylbenzoate synthase from Escherichia coli
Biochemistry
42
14427-14433
2003
Escherichia coli (P29208), Escherichia coli
Manually annotated by BRENDA team
Weische, A.; Garvert, W.; Leistner, E.
Biosynthesis of o-succinylbenzoic acid. II.: Properties of o-succinylbenzoic acid synthase, an enzyme involved in vitamin K2 biosynthesis
Arch. Biochem. Biophys.
256
223-231
1987
Escherichia coli, Escherichia coli AN 154
Manually annotated by BRENDA team
Zhu, W.W.; Wang, C.; Jipp, J.; Ferguson, L.; Lucas, S.N.; Hicks, M.A.; Glasner, M.E.
Residues required for activity in Escherichia coli o-succinylbenzoate synthase (OSBS) are not conserved in all OSBS enzymes
Biochemistry
51
6171-6181
2012
Escherichia coli
Manually annotated by BRENDA team
Odokonyero, D.; Ragumani, S.; Lopez, M.S.; Bonanno, J.B.; Ozerova, N.D.; Woodard, D.R.; Machala, B.W.; Swaminathan, S.; Burley, S.K.; Almo, S.C.; Glasner, M.E.
Divergent evolution of ligand binding in the o-succinylbenzoate synthase family
Biochemistry
52
7512-7521
2013
Escherichia coli (P29208), Escherichia coli, Thermobifida fusca (Q47Q21), Thermobifida fusca
Manually annotated by BRENDA team