Immobilization of Bacillus subtilis oxalate decarboxylase on a Zn-IMAC resin.

about

Immobilization of Bacillus subtilis oxalate decarboxylase on a Zn-IMAC resin.

Item

http://www.wikidata.org/entity/Q47103948

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年学术文章

@wuu

2015年学术文章

@zh

2015年学术文章

@zh-cn

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

@zh-hant

name

Immobilization of Bacillus subtilis oxalate decarboxylase on a Zn-IMAC resin.

@en

Immobilization of Bacillus subtilis oxalate decarboxylase on a Zn-IMAC resin.

@nl

type

Item

label

Immobilization of Bacillus subtilis oxalate decarboxylase on a Zn-IMAC resin.

@en

Immobilization of Bacillus subtilis oxalate decarboxylase on a Zn-IMAC resin.

@nl

prefLabel

Immobilization of Bacillus subtilis oxalate decarboxylase on a Zn-IMAC resin.

@en

Immobilization of Bacillus subtilis oxalate decarboxylase on a Zn-IMAC resin.

@nl

P1476

Immobilization of Bacillus subtilis oxalate decarboxylase on a Zn-IMAC resin.

@en

P2093

Andrew Ozarowski

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

Laura Molina

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

Umar Twahir

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

P2860

Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A resolution

A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site

The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site lid conformations 1

A Structural Element That Facilitates Proton-Coupled Electron Transfer in Oxalate Decarboxylase

Assigning the EPR Fine Structure Parameters of the Mn(II) Centers in Bacillus subtilis Oxalate Decarboxylase by Site-Directed Mutagenesis and DFT/MM Calculations

Oxalate decarboxylase requires manganese and dioxygen for activity. Overexpression and characterization of Bacillus subtilis YvrK and YoaN

Cupins: the most functionally diverse protein superfamily?

Phylogeny, function, and evolution of the cupins, a structurally conserved, functionally diverse superfamily of proteins.

Metal dependence of oxalate decarboxylase activity.

Perspectives of immobilized-metal affinity chromatography.

P304

98-103

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

P31

scholarly article

P356

10.1016/J.BBREP.2015.08.017

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

P478

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

P50

Alexander Angerhofer

P577

2015-08-28T00:00:00Z

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

P5875

282831465

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

P698

29124192

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

P932

5668902

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