Substrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels That Enable Long Chain Olefin Biosynthesis.

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Active Multienzyme Assemblies for Long-Chain Olefinic Hydrocarbon Biosynthesis.OleA Glu117 is key to condensation of two fatty-acyl coenzyme A substrates in long-chain olefin biosynthesis.The role of OleA His285 in orchestration of long-chain acyl-coenzyme A substrates.

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Substrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels That Enable Long Chain Olefin Biosynthesis.

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http://www.wikidata.org/entity/Q46463273

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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Substrate Trapping in Crystals ...... ong Chain Olefin Biosynthesis.

@en

Substrate Trapping in Crystals ...... ong Chain Olefin Biosynthesis.

@en-gb

Substrate Trapping in Crystals ...... ong Chain Olefin Biosynthesis.

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Item

label

Substrate Trapping in Crystals ...... ong Chain Olefin Biosynthesis.

@en

Substrate Trapping in Crystals ...... ong Chain Olefin Biosynthesis.

@en-gb

Substrate Trapping in Crystals ...... ong Chain Olefin Biosynthesis.

@nl

prefLabel

Substrate Trapping in Crystals ...... ong Chain Olefin Biosynthesis.

@en

Substrate Trapping in Crystals ...... ong Chain Olefin Biosynthesis.

@en-gb

Substrate Trapping in Crystals ...... ong Chain Olefin Biosynthesis.

@nl

P1476

Substrate Trapping in Crystals ...... ong Chain Olefin Biosynthesis.

@en

P2093

Brandon R Goblirsch

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

Fatuma A Mohamed

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P2860

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Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III

Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery

Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway

X-Ray Crystal Structure of Mycobacterium tuberculosis β-Ketoacyl Acyl Carrier Protein Synthase II (mtKasB)

Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH

Crystal Structures of Xanthomonas campestris OleA Reveal Features That Promote Head-to-Head Condensation of Two Long-Chain Fatty Acids

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26698-26706

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scholarly article

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10.1074/JBC.M116.760892

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English

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291

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Carrie M Wilmot

Matthew R Jensen

Lawrence P. Wackett

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2016-11-04T00:00:00Z

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27815501

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5207179

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Substrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels That Enable Long Chain Olefin Biosynthesis.

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P2860

P2860

Substrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels That Enable Long Chain Olefin Biosynthesis.

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type

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P1433

P1476

P2093

P2860

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P356

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P433

P478

P50

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P698

P932

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