2.3.1.46: homoserine O-succinyltransferase
This is an abbreviated version!
For detailed information about homoserine O-succinyltransferase, go to the full flat file.
Word Map on EC 2.3.1.46
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2.3.1.46
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chaperone
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acyltransferases
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refolding
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noncanonical
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cereus
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threonine
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biotechnology
- 2.3.1.46
- chaperone
- acyltransferases
-
refolding
-
noncanonical
- cereus
- threonine
- biotechnology
Reaction
Synonyms
homoserine O-succinyltransferase, homoserine O-transsuccinylase, homoserine succinyltransferase, homoserine transsuccinylase, homoserine-O-succinyltransferase, HST, HTS, MetA, MetA protein, succinyltransferase, homoserine
ECTree
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Reaction
Reaction on EC 2.3.1.46 - homoserine O-succinyltransferase
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ping-pong mechanism, enzyme contains a cysteine in the active site, member of the acyltransferase family
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succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine
succinyl is covalently bound to one of two adjacent lysine residues at positions 45 and 46
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succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine
ping pong catalytic reaction mechanism, roles of essential functional groups, the catalytic triad is formed by the nucleophile Cys142, the essential base His235, and Glu237, required for proper orientation of His235, Lys46 is required for interaction with succinyl-CoA, and Arg193 is involved in binding of L-Homoserine
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succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine
ping pong catalytic reaction mechanism, the residues Cys142, His235, and Lys47 are essential for catalytic activity, Cys142 acts as nucleophile to which the succinyl moiety is transferred during the reaction followed by transfer to homoserine to form O-succinylhomoserine, Lys47 is involved in the first half-reaction, and His235 is the active site base
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