Enzyme

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EC Tree
     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.238
Description:Monacolin J acid methylbutanoate transferase.
Cath: 3.40.710.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.238
BRENDA Enzyme Link: BRENDA 2.3.1.238
KEGG Enzyme Link: KEGG2.3.1.238
BioCyc Enzyme Link: BioCyc 2.3.1.238
ExPASy Enzyme Link: ExPASy2.3.1.238
EC2PDB Enzyme Link: EC2PDB 2.3.1.238
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.238
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.238
IntEnz Enzyme Link: IntEnz 2.3.1.238
MEDLINE Enzyme Link: MEDLINE 2.3.1.238
MSA:

2.3.1.238;

Phylogenetic Tree:

2.3.1.238;

Uniprot:
M-CSA:
RHEA:43064 (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + monacolin J carboxylate = holo-[2-methylbutanoate polyketide synthase] + lovastatin carboxylate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S;H0;+0:4]-[C;H0;+0:5](=[*:6])-[*:7]>>[*:3]-[SH;+0:4].[*:6]=[C;H0;+0:5](-[*:7])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis.Kennedy J, Auclair K, Kendrew SG, Park C, Vederas JC, Hutchinson CR1999 May 2110334994
Directed evolution and structural characterization of a simvastatin synthase.Gao X, Xie X, Pashkov I, Sawaya MR, Laidman J, Zhang W, Cacho R, Yeates TO, Tang Y2009 Oct 3019875080
Acyltransferase mediated polyketide release from a fungal megasynthase.Xie X, Meehan MJ, Xu W, Dorrestein PC, Tang Y2009 Jun 2419530726
Rational improvement of simvastatin synthase solubility in Escherichia coli leads to higher whole-cell biocatalytic activity.Xie X, Pashkov I, Gao X, Guerrero JL, Yeates TO, Tang Y2009 Jan 118988191
Biosynthesis of lovastatin analogs with a broadly specific acyltransferase.Xie X, Watanabe K, Wojcicki WA, Wang CC, Tang Y2006 Nov17113998