Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ.

about

Nonribosomal peptide synthetase biosynthetic clusters of ESKAPE pathogens.The biosynthesis of pyoverdines

P2860

Q39392982-8D36C846-0037-4AA5-89BB-A0670FB75A47 Q58564188-8A6428E9-5C02-4BDE-826C-50EF097DE9DD

P2860

Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ.

Item

http://www.wikidata.org/entity/Q38758925

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

2017年论文

@zh

2017年论文

@zh-cn

name

Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ.

@en

type

Item

label

Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ.

@en

prefLabel

Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ.

@en

P1476

Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ

@en

P2093

Daniel Catlin

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

Eric J Drake

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

Kenneth D Clevenger

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

Romila Mascarenhas

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

Rui Wu

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

P2860

Circular permutation: a different way to engineer enzyme structure and function

FpvA bound to non-cognate pyoverdines: molecular basis of siderophore recognition by an iron transporter

The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket

Structures of an isopenicillin N converting Ntn-hydrolase reveal different catalytic roles for the active site residues of precursor and mature enzyme

Two Structures of an N-Hydroxylating Flavoprotein Monooxygenase: ORNITHINE HYDROXYLASE FROM PSEUDOMONAS AERUGINOSA

Uncoupling Intramolecular Processing and Substrate Hydrolysis in the N-Terminal Nucleophile Hydrolase hASRGL1 by Circular Permutation

Structural Characterization and High-Throughput Screening of Inhibitors of PvdQ, an NTN Hydrolase Involved in Pyoverdine Synthesis

Rational design of a transition state analogue with picomolar affinity for Pseudomonas aeruginosa PvdQ, a siderophore biosynthetic enzyme

n-Alkylboronic acid inhibitors reveal determinants of ligand specificity in the quorum-quenching and siderophore biosynthetic enzyme PvdQ

The Cationminus signpi Interaction

P304

643-647

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

P31

scholarly article

P356

10.1021/ACSCHEMBIO.7B00031

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

P433

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

P478

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

P50

P577

2017-02-15T00:00:00Z

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

P698

28186406

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

P932

5373092

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

Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ.

about

P2860

P2860

Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932