Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase
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Mycocerosic acid synthase exemplifies the architecture of reducing polyketide synthasesDomain Organization and Active Site Architecture of a Polyketide Synthase C-methyltransferaseVinylogous Dehydration by a Polyketide Dehydratase Domain in Curacin Biosynthesis.The Structural Relationship between Iterative and Modular PKSs.A conserved threonine prevents self-intoxication of enoyl-thioester reductases.Mechanistic insight into acrylate metabolism and detoxification in marine dimethylsulfoniopropionate-catabolizing bacteria.PKS-NRPS Enzymology and Structural Biology: Considerations in Protein Production.InhA, the enoyl-thioester reductase from forms a covalent adduct during catalysis
P2860
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P2860
Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase
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2015 nî lūn-bûn
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2015年の論文
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2015年学术文章
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name
Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase
@ast
Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase
@en
type
label
Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase
@ast
Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase
@en
prefLabel
Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase
@ast
Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase
@en
P2093
P2860
P1433
P1476
Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase
@en
P2093
David H Sherman
Dheeraj Khare
Janet L Smith
Liangcai Gu
Wendi A Hale
William H Gerwick
P2860
P304
P356
10.1016/J.STR.2015.09.013
P577
2015-10-24T00:00:00Z