Identification of Middle Chain Fatty Acyl-CoA Ligase Responsible for the Biosynthesis of 2-Alkylmalonyl-CoAs for Polyketide Extender Unit.

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A crotonyl-CoA reductase-carboxylase independent pathway for assembly of unusual alkylmalonyl-CoA polyketide synthase extender units.In silico identification of lysocin biosynthetic gene cluster from Lysobacter sp. RH2180-5.

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Q37533520-6F16B94E-639E-406D-BDF1-0015BEB7E817 Q54499750-010C5ACA-AFEE-4464-B307-D1703F9BA900

P2860

Identification of Middle Chain Fatty Acyl-CoA Ligase Responsible for the Biosynthesis of 2-Alkylmalonyl-CoAs for Polyketide Extender Unit.

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http://www.wikidata.org/entity/Q40531171

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

@yue

2015年論文

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2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

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2015年论文

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2015年论文

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name

Identification of Middle Chain ...... for Polyketide Extender Unit.

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type

Item

label

Identification of Middle Chain ...... for Polyketide Extender Unit.

@en

prefLabel

Identification of Middle Chain ...... for Polyketide Extender Unit.

@en

P1476

Identification of Middle Chain ...... s for Polyketide Extender Unit

@en

P2093

Akihiro Kawata

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

Hiroyuki Osada

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Shunji Takahashi

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

Takeshi Miyazawa

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Takeshi Shimizu

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Teruo Hayashi

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Toshihiko Nogawa

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P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase

Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway

Mechanistic and functional insights into fatty acid activation in Mycobacterium tuberculosis

Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila

Unusual carbon fixation gives rise to diverse polyketide extender units

Structures of Mycobacterium tuberculosis FadD10 Protein Reveal a New Type of Adenylate-forming Enzyme

One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products

Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA Synthetase (FadD13) of Mycobacterium tuberculosis

Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis

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26994-27011

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scholarly article

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10.1074/JBC.M115.677195

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English

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

P478

290

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Suresh Panthee

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2015-09-16T00:00:00Z

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P698

26378232

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P932

4646404

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Identification of Middle Chain Fatty Acyl-CoA Ligase Responsible for the Biosynthesis of 2-Alkylmalonyl-CoAs for Polyketide Extender Unit.

about

P2860

P2860

Identification of Middle Chain Fatty Acyl-CoA Ligase Responsible for the Biosynthesis of 2-Alkylmalonyl-CoAs for Polyketide Extender Unit.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932