Tyrosine O-prenyltransferases TyrPT and SirD displaying similar behavior toward unnatural alkyl or benzyl diphosphate as their natural prenyl donor dimethylallyl diphosphate.

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Impacts and perspectives of prenyltransferases of the DMATS superfamily for use in biotechnology.Determination of Alkyl-Donor Promiscuity of Tyrosine-O-Prenyltransferase SirD from Leptosphaeria maculans.

P2860

Q38557858-75413E6D-A6F1-4E8A-B826-49B8C330ECA8 Q47726863-17D93458-9DE3-47B8-A308-459008F716C2

P2860

Tyrosine O-prenyltransferases TyrPT and SirD displaying similar behavior toward unnatural alkyl or benzyl diphosphate as their natural prenyl donor dimethylallyl diphosphate.

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http://www.wikidata.org/entity/Q46738299

description

2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

@wuu

2015年学术文章

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2015年学术文章

@zh-hans

2015年学术文章

@zh-my

2015年学术文章

@zh-sg

2015年學術文章

@yue

2015年學術文章

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2015年學術文章

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name

Tyrosine O-prenyltransferases ...... nor dimethylallyl diphosphate.

@en

Tyrosine O-prenyltransferases ...... nor dimethylallyl diphosphate.

@nl

type

Item

label

Tyrosine O-prenyltransferases ...... nor dimethylallyl diphosphate.

@en

Tyrosine O-prenyltransferases ...... nor dimethylallyl diphosphate.

@nl

prefLabel

Tyrosine O-prenyltransferases ...... nor dimethylallyl diphosphate.

@en

Tyrosine O-prenyltransferases ...... nor dimethylallyl diphosphate.

@nl

P1476

Tyrosine O-prenyltransferases ...... nor dimethylallyl diphosphate.

@en

P2093

Huili Yu

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

Mike Liebhold

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

Shu-Ming Li

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

Xiulan Xie

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

P2860

Identification of the viridicatumtoxin and griseofulvin gene clusters from Penicillium aethiopicum

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Prenyl transfer to aromatic substrates: genetics and enzymology.

Discovery and characterization of a group of fungal polycyclic polyketide prenyltransferases.

Prenylation of aromatic compounds, a key diversification of plant secondary metabolites.

Prenylated indole derivatives from fungi: structure diversity, biological activities, biosynthesis and chemoenzymatic synthesis.

Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides.

Tyrosine derivatives isolated from Streptomyces sp. IFM 10937 in a screening program for TRAIL-resistance-overcoming activity.

Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on tyrosine and tryptophan derivatives

Site-directed mutagenesis switching a dimethylallyl tryptophan synthase to a specific tyrosine C3-prenylating enzyme.

P2888

s00253-015-6452-1

P304

7115-7124

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scholarly article

P356

10.1007/S00253-015-6452-1

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English

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P478

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

P577

2015-02-24T00:00:00Z

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P5875

272844242

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25707862

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Tyrosine O-prenyltransferases TyrPT and SirD displaying similar behavior toward unnatural alkyl or benzyl diphosphate as their natural prenyl donor dimethylallyl diphosphate.

about

P2860

P2860

Tyrosine O-prenyltransferases TyrPT and SirD displaying similar behavior toward unnatural alkyl or benzyl diphosphate as their natural prenyl donor dimethylallyl diphosphate.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P577

P5875

P698