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2.3.1.199: very-long-chain 3-oxoacyl-CoA synthase

This is an abbreviated version!
For detailed information about very-long-chain 3-oxoacyl-CoA synthase, go to the full flat file.

Word Map on EC 2.3.1.199

Reaction

a very-long-chain acyl-CoA
+
malonyl-CoA
=
a very-long-chain 3-oxoacyl-CoA
 +
CO2
 +
CoA

Synonyms

3-ketoacyl CoA synthase, 3-ketoacyl-CoA synthase, acyl-CoA elongase, At1g01120, At2g26640, beta-ketoacyl CoA synthase, beta-ketoacyl-CoA synthase, Cer-zh, CER2-LIKE1, CER2-LIKE2, CER26, CER26L, CER6, CER60, condensing enzyme, Cut1, CUT1L, EC 2.3.1.119, ECERIFERUM 26, ECERIFERUM 26-like, ELO, ELo1, Elo1p, Elo2p, Elo3p, EloA, ELOVL1, ELOVL5, Elovl6, ELOVL7, FA elongase, FAE1, FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS, Fatty acid elongase, fatty acid elongase 1, fatty acid elongation 1, fatty acid elongation1, KCS, Kcs1, KCS17, KCS2, KCS2/DAISY, KCS20, MALCE1, microsomal fatty acid elongase, Onion2, Os03g0220100, Os10 g0416200, seed-specific condensing enzyme, very-long-chain fatty acid condensing enzyme, very-long-chain fatty acid-condensing enzyme, VLCFA condensing enzyme, VLCFA elongase, WSL4

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.199 very-long-chain 3-oxoacyl-CoA synthase

Engineering

Engineering on EC 2.3.1.199 - very-long-chain 3-oxoacyl-CoA synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C223A
-
the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present
H391A
-
the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present
H391K
-
the mutant shows very low condensation activity
H391Q
-
the mutant shows low condensation activity (25% activity compared to the wild type enzyme)
N424D
-
the mutant shows low condensation activity
N424H
-
the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present
S282A
-
the mutant shows reduced activity with 20:1DELTA11 and erucic acid-CoA as substrates compared to the wild type enzyme
S282C
-
the mutant shows increased activity with 20:1DELTA11 and erucic acid-CoA as substrates compared to the wild type enzyme
S282G
-
the mutant shows wild type activity with 20:1DELTA11 and erucic acid-CoA as substrates
S282I
-
the mutant is inactive
S282N
-
the mutant is inactive
S282Q
-
the mutant is inactive
S282T
-
the mutant shows reduced activity with 20:1DELTA11 and erucic acid-CoA as substrates compared to the wild type enzyme
S282V
-
the mutant is inactive
S282Y
-
the mutant is inactive
additional information