Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity. - Test2 - elhamkhani - TriplyDB

Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity.

Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity.

http://www.wikidata.org/entity/Q43069253

about

Structural Insight into the Tetramerization of an Iterative Ketoreductase SiaM through Aromatic Residues in the Interfaces Inhibition Kinetics and Emodin Cocrystal Structure of a Type II Polyketide Ketoreductase † , ‡Crystal structure and functional analysis of tetracenomycin ARO/CYC: Implications for cyclization specificity of aromatic polyketides Structural and Biochemical Analyses of Regio- and Stereospecificities Observed in a Type II Polyketide Ketoreductase Structural and Biochemical Studies of the Hedamycin Type II Polyketide Ketoreductase ( Hed KR): Molecular Basis of Stereo- and Regiospecificities The Determinants of Activity and Specificity in Actinorhodin Type II Polyketide Ketoreductase Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum Structural enzymology of polyketide synthases.Cyclization of aromatic polyketides from bacteria and fungi Modeling holo-ACP:DH and holo-ACP:KR complexes of modular polyketide synthases: a docking and molecular dynamics study.Modeling linear and cyclic PKS intermediates through atom replacement.Biosynthesis of colabomycin E, a new manumycin-family metabolite, involves an unusual chain-length factor.The type I fatty acid and polyketide synthases: a tale of two megasynthases Type II polyketide synthases: gaining a deeper insight into enzymatic teamwork.Structural insights into nonribosomal peptide enzymatic assembly lines Biosynthesis of aromatic polyketides in bacteria.iso-Migrastatin, migrastatin, and dorrigocin production in Streptomyces platensis NRRL 18993 is governed by a single biosynthetic machinery featuring an acyltransferase-less type I polyketide synthase.The structural role of the carrier protein--active controller or passive carrier.Substrate-Assisted Catalysis in Polyketide Reduction Proceeds via a Phenolate Intermediate Redirecting the cyclization steps of fungal polyketide synthase.A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase.Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase.In vivo and in vitro analysis of the hedamycin polyketide synthase.Investigation of early tailoring reactions in the oxytetracycline biosynthetic pathway.

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P2860

Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity.

http://www.wikidata.org/entity/Q43069253

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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Structural analysis of actinor ...... ing and substrate specificity.

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Structural analysis of actinor ...... ing and substrate specificity.

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Structural analysis of actinor ...... ing and substrate specificity.

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Structural analysis of actinor ...... ing and substrate specificity.

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Structural analysis of actinor ...... ing and substrate specificity.

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Structural analysis of actinor ...... ing and substrate specificity.

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Structural analysis of actinor ...... ing and substrate specificity.

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Jason Anthony Hill

http://www.w3.org/2001/XMLSchema#string

Shiou-Chuan Tsai

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Thanh Nhat Vu

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Tyler Paz Korman

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P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

The X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis

Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 A resolution

Structures of trihydroxynaphthalene reductase-fungicide complexes: implications for structure-based design and catalysis

Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis

Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis

Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2)

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14529-14538

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10.1021/BI048133A

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