Synthesis of bacillithiol and the catalytic selectivity of FosB-type fosfomycin resistance proteins - Wikidata - wikimedia - TriplyDB

Synthesis of bacillithiol and the catalytic selectivity of FosB-type fosfomycin resistance proteins

Synthesis of bacillithiol and the catalytic selectivity of FosB-type fosfomycin resistance proteins

http://www.wikidata.org/entity/Q36530848

about

Bacillithiol: a key protective thiol in Staphylococcus aureus Structural and Chemical Aspects of Resistance to the Antibiotic Fosfomycin Conferred by FosB from Bacillus cereus Structure and Function of the Genomically Encoded Fosfomycin Resistance Enzyme, FosB, from Staphylococcus aureus Redox regulation by reversible protein S-thiolation in bacteria Mechanistic studies of FosB: a divalent-metal-dependent bacillithiol-S-transferase that mediates fosfomycin resistance in Staphylococcus aureus.X-ray crystallographic structure of BshC, a unique enzyme involved in bacillithiol biosynthesis.Protective role of bacillithiol in superoxide stress and Fe-S metabolism in Bacillus subtilis.Purification and characterization of the Staphylococcus aureus bacillithiol transferase BstA Importance of bacillithiol in the oxidative stress response of Staphylococcus aureus.The Role of Bacillithiol in Gram-Positive Firmicutes.Lack of formylated methionyl-tRNA has pleiotropic effects on Bacillus subtilis.Staphylococcus aureus CstB Is a Novel Multidomain Persulfide Dioxygenase-Sulfurtransferase Involved in Hydrogen Sulfide Detoxification.Impact of antibiotics with various target sites on the metabolome of Staphylococcus aureus.A Structural, Functional, and Computational Analysis of BshA, the First Enzyme in the Bacillithiol Biosynthesis Pathway.Structure and Function of the Bacillithiol-S-Transferase BstA from Staphylococcus aureus.

P2860

Q26799816-5401946E-B8AB-46F1-9F98-D9C93DAF70BA Q27679869-3569D20F-152E-44C4-B72E-AE0B962A5D67 Q27681408-BBC8F982-684F-4E6D-A5BA-F20F2EE31C34 Q28083854-C8ADCD29-CC44-452F-8882-F3464D1C9B3B Q34318798-4C4BF443-98B1-4F22-815E-0D38781863DF Q35001116-87E3F969-72D9-4F12-9179-0926EB09874C Q36010473-5A012811-88D8-43F3-8D9D-198CB38B6263 Q36715365-F1158A3D-EDC5-4272-AAE7-A3C5DF2A2761 Q37548104-1BF0FF45-E483-4B07-B1E0-801AFF6E1FED Q38744009-5A52780C-67DA-4BE6-986D-2990BCD76A0B Q39095175-FE83D852-5B1A-49D9-A0AA-1EB86BBF2C36 Q40734216-4EA13316-4D09-4C93-92AC-55E05851735D Q43045895-9797D5DB-CCE8-41A5-BAE1-6F6C34C2FF2B Q46511700-09E7820A-CD65-4D59-B45C-CB91443B44FF Q50124896-0C726C51-F81A-4E67-A669-209BAAEC990E

P2860

Synthesis of bacillithiol and the catalytic selectivity of FosB-type fosfomycin resistance proteins

http://www.wikidata.org/entity/Q36530848

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Synthesis of bacillithiol and ...... fosfomycin resistance proteins

@ast

Synthesis of bacillithiol and ...... fosfomycin resistance proteins

@en

type

label

Synthesis of bacillithiol and ...... fosfomycin resistance proteins

@ast

Synthesis of bacillithiol and ...... fosfomycin resistance proteins

@en

prefLabel

Synthesis of bacillithiol and ...... fosfomycin resistance proteins

@ast

Synthesis of bacillithiol and ...... fosfomycin resistance proteins

@en

P1433

Q36530848-52586AD6-89D8-4263-9D6A-D8B2456A8703

P1476

Q36530848-2E1DD8DB-C200-4CEA-878A-B000EE79431F

P2093

Q36530848-0A28956C-E14D-4695-B084-4AD8DDDDC1D7

Q36530848-12752AA6-7CE7-4BC5-A908-2456A0217B48

Q36530848-391E8140-DC37-40A9-A498-B04FA617FFFA

Q36530848-3C10924D-9AC0-400A-B83D-D11CC44ABC7E

Q36530848-3E462735-E682-4F64-89E2-7A59707DAC33

Q36530848-5A8D22FD-AC60-417E-A366-B72449E984D8

Q36530848-8FA25E6E-E547-4203-8E90-5743598897ED

Q36530848-C58E95F3-54B5-4D91-8915-0D85128BFA51

P2860

Q36530848-0F10DB34-378C-4100-B9AD-9BCAC101C83B

Q36530848-15563A3B-5463-4C2B-8D8D-316303D6F007

Q36530848-230D0AFB-3558-4668-8E1C-E93E06F3BCFF

Q36530848-38E431AE-4411-40ED-88BF-6F8CBF76E646

Q36530848-4C53C9A3-FA70-42F9-8E23-3B6F2E7CA367

Q36530848-4E656C9F-2ED6-421E-BABD-8CE802B73473

Q36530848-600D8B6A-B96E-433F-90D1-7CF495525B01

Q36530848-741419A5-BB11-4893-9C8A-1EF4B81C97EF

Q36530848-7490E9AE-8182-4913-A065-ACB5BD00F245

Q36530848-85405180-B11B-47E5-BA01-89FE65CA262D

P304

Q36530848-20F60A20-B50A-406C-804A-7E408C4C05A1

P31

Q36530848-32B7B4FB-8134-4A73-829D-EE952855FAC9

P356

Q36530848-F9D98614-AF5E-4E73-86E8-FFD06DF8C246

P407

Q36530848-EFA13B2C-320E-428C-AF86-6980FD496B63

P433

Q36530848-6D63ABE0-BCF3-4A4A-B504-F2C9168C8FFB

P478

Q36530848-0069AC87-7EC0-4F6F-B7FC-EEE683AC3A34

P577

Q36530848-4849FF90-773D-4A21-BACE-259EE074C201

P698

Q36530848-7A805A59-29EA-453C-9C43-47ADD1A74226

P921

Q36530848-C06107E0-58D7-48AF-B47A-FF4DEDB96909

P932

Q36530848-01D87A8F-6799-4A59-B2BF-B93F5C3D964E

P356

P1433

Organic Letters

P1476

Synthesis of bacillithiol and ...... fosfomycin resistance proteins

@en

P2093

Alexander P Lamers

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

Donald F Stec

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

Gary A Sulikowski

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

Kelly M Hines

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

Kwangho Kim

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

Mary E Keithly

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

Paul D Cook

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

Richard N Armstrong

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

P2860

Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli

Bacillithiol is an antioxidant thiol produced in Bacilli

FosB, a cysteine-dependent fosfomycin resistance protein under the control of sigma(W), an extracytoplasmic-function sigma factor in Bacillus subtilis

Novel thiols of prokaryotes.

Characterization of the N-acetyl-α-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis .

Chemical and Chemoenzymatic syntheses of bacillithiol: a unique low-molecular-weight thiol amongst low G + C Gram-positive bacteria.

Fosfomycin resistance proteins: a nexus of glutathione transferases and epoxide hydrolases in a metalloenzyme superfamily.

Activity-guided identification of (S)-malic acid 1-O-D-glucopyranoside (morelid) and gamma-aminobutyric acid as contributors to umami taste and mouth-drying oral sensation of morel mushrooms (Morchella deliciosa Fr.).

Bacillithiol, a new player in bacterial redox homeostasis.

The many faces of glutathione in bacteria.

P304

5207-5209

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

P31

scholarly article

P356

10.1021/OL302327T

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

P407

P433

20

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

P478

14

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

P577

2012-10-03T00:00:00Z

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

P698

23030527

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

P921

P932

3544479

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