6.2.1.26: O-succinylbenzoate-CoA ligase
This is an abbreviated version!
For detailed information about O-succinylbenzoate-CoA ligase, go to the full flat file.
Word Map on EC 6.2.1.26
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6.2.1.26
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menaquinone
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o-succinylbenzoic
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1,4-dihydroxy-2-naphthoic
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half-reaction
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drug development
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anthracis
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semi-automated
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wells
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5'-triphosphate
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mono-phosphate
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adenylyltransferase
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phylloquinone
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backside
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benzoic
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mononucleotide
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phlei
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dihydroxynaphthoate
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in-line
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unattended
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ping-pong
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isochorismate
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ultra-high
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thioesterification
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scalable
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liquid-handling
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malachite
- 6.2.1.26
- menaquinone
-
o-succinylbenzoic
-
1,4-dihydroxy-2-naphthoic
-
half-reaction
- drug development
- anthracis
-
semi-automated
-
wells
- 5'-triphosphate
-
mono-phosphate
- adenylyltransferase
- phylloquinone
-
backside
-
benzoic
- mononucleotide
- phlei
-
dihydroxynaphthoate
-
in-line
-
unattended
-
ping-pong
- isochorismate
-
ultra-high
-
thioesterification
-
scalable
-
liquid-handling
- malachite
Reaction
Synonyms
AAE14, acyl-activating enzyme 14, BsMenE, MenE, O-succinylbenzoate-CoA synthase, o-succinylbenzoate-CoA synthetase, o-succinylbenzoyl-CoA synthetase, o-succinylbenzoyl-coenzyme A ligase, o-succinylbenzoyl-coenzyme A synthetase, OSB-CoA ligase, OSB-CoA synthetase, OSB:CoA ligase, synthetase, o-succinylbenzoyl coenzyme A
ECTree
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General Information
General Information on EC 6.2.1.26 - O-succinylbenzoate-CoA ligase
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metabolism
physiological function
additional information
o-succinylbenzoyl-CoA synthetase, or MenE, is an essential adenylate-forming enzyme in the menaquinone biosynthesis
metabolism
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o-succinylbenzoyl-CoA synthetase, or MenE, is an essential adenylate-forming enzyme in the menaquinone biosynthesis
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the enzyme is essential in Escherichia coli and is involved in menaquinone biosynthesis
physiological function
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the enzyme is essential in Mycobacterium tuberculosis and is involved in menaquinone biosynthesis
physiological function
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the enzyme is important in Mycobacterium tuberculosis
physiological function
ATP-dependent configuration of adenylation active site in o-succinylbenzoyl-CoA synthetase
physiological function
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ATP-dependent configuration of adenylation active site in o-succinylbenzoyl-CoA synthetase
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the basic residue, Arg222, may interact with the aromatic carboxylate of 2-succinylbenzoate
additional information
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the basic residue, Arg222, may interact with the aromatic carboxylate of 2-succinylbenzoate
additional information
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the basic residue, Arg222, may interact with the aromatic carboxylate of 2-succinylbenzoate
additional information
in MenE catalysis, tight gripping interactions of the phosphate-binding loop (P-loop) with the ATP triphosphate moiety and an open-closed conformational change to form a compact adenylation active site create a new binding site for the carboxylate substrate, allowing revelation of the determinants of substrate specificities and in-line alignment of the two substrates for backside nucleophilic substitution reaction by molecular modeling, overview. The ATP-enzyme interaction is suggested to play a crucial catalytic role. positioning and catalytic role of a conserved lysine residue in stabilization of the transition state, molecular docking, overview
additional information
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in MenE catalysis, tight gripping interactions of the phosphate-binding loop (P-loop) with the ATP triphosphate moiety and an open-closed conformational change to form a compact adenylation active site create a new binding site for the carboxylate substrate, allowing revelation of the determinants of substrate specificities and in-line alignment of the two substrates for backside nucleophilic substitution reaction by molecular modeling, overview. The ATP-enzyme interaction is suggested to play a crucial catalytic role. positioning and catalytic role of a conserved lysine residue in stabilization of the transition state, molecular docking, overview
additional information
-
in MenE catalysis, tight gripping interactions of the phosphate-binding loop (P-loop) with the ATP triphosphate moiety and an open-closed conformational change to form a compact adenylation active site create a new binding site for the carboxylate substrate, allowing revelation of the determinants of substrate specificities and in-line alignment of the two substrates for backside nucleophilic substitution reaction by molecular modeling, overview. The ATP-enzyme interaction is suggested to play a crucial catalytic role. positioning and catalytic role of a conserved lysine residue in stabilization of the transition state, molecular docking, overview
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