Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

about

Uncovering the Catalytic Direction of Chondroitin AC Exolyase: FROM THE REDUCING END TOWARDS THE NON-REDUCING END De novo synthesis of a narrow size distribution low-molecular-weight heparin.

P2860

Q36744482-B0BD35BE-47BB-4211-8961-87525BA27088 Q37685686-87E69285-7B35-4250-8E4C-2DC4421022C8

P2860

Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

Item

http://www.wikidata.org/entity/Q36419362

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年学术文章

@wuu

2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

2012年學術文章

@zh

2012年學術文章

@zh-hant

name

Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

@ast

Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

@en

type

Item

label

Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

@ast

Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

@en

prefLabel

Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

@ast

Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

@en

P1476

Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

@en

P2093

Jian Liu

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

Timothy R O'Leary

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

Yongmei Xu

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

P2860

Crystal structure of Escherichia coli phage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related

The K5 Lyase KflA Combines a Viral Tail Spike Structure with a Bacterial Polysaccharide Lyase Mechanism

Mass spectrometric evidence for the enzymatic mechanism of the depolymerization of heparin-like glycosaminoglycans by heparinase II.

Direct evidence for a predominantly exolytic processive mechanism for depolymerization of heparin-like glycosaminoglycans by heparinase I.

Using an enzymatic combinatorial approach to identify anticoagulant heparan sulfate structures.

Chemoenzymatic design of heparan sulfate oligosaccharides

Unraveling the specificity of heparanase utilizing synthetic substrates.

Enzymatic redesigning of biologically active heparan sulfate.

Glycomics approach to structure-function relationships of glycosaminoglycans.

Expression of heparan sulfate sulfotransferases in Kluyveromyces lactis and preparation of 3'-phosphoadenosine-5'-phosphosulfate.

P304

132-141

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

P31

scholarly article

P356

10.1093/GLYCOB/CWS136

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

P433

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

P478

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

P577

2012-09-26T00:00:00Z

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

P698

23019155

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

P921

bacteriophage

P932

3505012

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

Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

about

P2860

P2860

Investigation of the substrate specificity of K5 lyase A from K5A bacteriophage

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P921

P932