Substrate-Assisted Catalysis in Polyketide Reduction Proceeds via a Phenolate Intermediate

scientific article published on 7 September 2016

Substrate-Assisted Catalysis in Polyketide Reduction Proceeds via a Phenolate Intermediate is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.CHEMBIOL.2016.07.018
P932PMC publication ID5039031
P698PubMed publication ID27617849

P50authorMartin SchäferQ39401461
Mark J ButtnerQ55764039
P2093author name stringBarrie Wilkinson
Clare E M Stevenson
David M Lawson
P2860cites workMedium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymesQ24642281
Substrate-assisted catalysis: molecular basis and biological significanceQ24672568
Inhibition Kinetics and Emodin Cocrystal Structure of a Type II Polyketide Ketoreductase † , ‡Q27649562
Crystal structure of a new type of NADPH-dependent quinone oxidoreductase (QOR2) from Escherichia coliQ27650522
Structural insight into bioremediation of triphenylmethane dyes by Citrobacter sp. triphenylmethane reductaseQ27652068
A crystal structure of the bifunctional antibiotic simocyclinone D8, bound to DNA gyraseQ27658456
Structures of the TetR-like simocyclinone efflux pump repressor, SimR, and the mechanism of ligand-mediated derepressionQ27666812
Structural and Biochemical Analyses of Regio- and Stereospecificities Observed in a Type II Polyketide KetoreductaseQ27667477
Structural and Biochemical Studies of the Hedamycin Type II Polyketide Ketoreductase ( Hed KR): Molecular Basis of Stereo- and RegiospecificitiesQ27670915
The Determinants of Activity and Specificity in Actinorhodin Type II Polyketide KetoreductaseQ27679936
A New Crystal Structure of the Bifunctional Antibiotic Simocyclinone D8 Bound to DNA Gyrase Gives Fresh Insight into the Mechanism of InhibitionQ27681978
Structural and functional analysis of angucycline C-6 ketoreductase LanV involved in landomycin biosynthesisQ27685213
Structure-based engineering of angucyclinone 6-ketoreductasesQ27695588
Angucyclinones from an Indonesian Streptomyces sp.Q33310451
Biosynthetic gene cluster of simocyclinone, a natural multihybrid antibioticQ34107244
Exploiting bacterial DNA gyrase as a drug target: current state and perspectives.Q34214929
Angucyclines: Biosynthesis, mode-of-action, new natural products, and synthesisQ37970299
Grisemycin, a Bridged Angucyclinone with a Methylsulfinyl Moiety from a Marine-Derived Streptomyces sp.Q38787683
Kiamycin, a unique cytotoxic angucyclinone derivative from a marine Streptomyces sp.Q39345356
SimC7 Is a Novel NAD(P)H-Dependent Ketoreductase Essential for the Antibiotic Activity of the DNA Gyrase Inhibitor Simocyclinone.Q41518213
Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificityQ43069253
Classification and nomenclature of the superfamily of short-chain dehydrogenases/reductases (SDRs).Q48629459
Classification of the short-chain dehydrogenase/reductase superfamily using hidden Markov modelsQ48662216
Simocyclinones, novel cytostatic angucyclinone antibiotics produced by Streptomyces antibioticus Tü 6040. I. Taxonomy, fermentation, isolation and biological activitiesQ48744539
Mass Spectrometry Reveals That the Antibiotic Simocyclinone D8 Binds to DNA Gyrase in a “Bent-Over” Conformation: Evidence of Positive Cooperativity in BindingQ58299773
Simocyclinones: diversity of metabolites is dependent on fermentation conditionsQ77460135
P433issue9
P304page(s)1091-1097
P577publication date2016-09-08
P1433published inCell Chemical BiologyQ27727180
P1476titleSubstrate-Assisted Catalysis in Polyketide Reduction Proceeds via a Phenolate Intermediate
P478volume23

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cites work (P2860)
Q39181168New insights into bacterial type II polyketide biosynthesis.
Q57801131Structural biology of 11-retinaldehyde production in the classical visual cycle
Q46263843Structural insights into simocyclinone as an antibiotic, effector ligand, and substrate
Q56888762The architectures of iterative type I PKS and FAS

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