Contribution of K99 and D319 to substrate binding and catalysis in the saccharopine dehydrogenase reaction

about

Evidence in Support of Lysine 77 and Histidine 96 as Acid–Base Catalytic Residues in Saccharopine Dehydrogenase from Saccharomyces cerevisiae

P2860

Q27676720-99012EBE-5BD6-4434-8530-D6C927A0731F

P2860

Contribution of K99 and D319 to substrate binding and catalysis in the saccharopine dehydrogenase reaction

Item

http://www.wikidata.org/entity/Q38480053

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Contribution of K99 and D319 t ...... aropine dehydrogenase reaction

@en

type

Item

label

Contribution of K99 and D319 t ...... aropine dehydrogenase reaction

@en

prefLabel

Contribution of K99 and D319 t ...... aropine dehydrogenase reaction

@en

P1476

Contribution of K99 and D319 t ...... aropine dehydrogenase reaction

@en

P2093

Ann H West

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

Devi K Ekanayake

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

Paul F Cook

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

P2860

The α-Aminoadipate Pathway for Lysine Biosynthesis in Fungi

Structural studies of the final enzyme in the alpha-aminoadipate pathway-saccharopine dehydrogenase from Saccharomyces cerevisiae

Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae

alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes.

Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae.

Lysine biosynthesis and metabolism in fungi

Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts.

Lysine biosynthesis in selected pathogenic fungi: characterization of lysine auxotrophs and the cloned LYS1 gene of Candida albicans.

Lysine biosynthesis pathway and biochemical blocks of lysine auxotrophs of Schizosaccharomyces pombe.

Statistical analysis of enzyme kinetic data.

P304

8-15

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

P31

scholarly article

P356

10.1016/J.ABB.2011.07.013

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

P407

English

P433

1-2

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

P478

514

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

P577

2011-07-27T00:00:00Z

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

P5875

51550458

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

P698

21819960

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

P932

3174770

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

Contribution of K99 and D319 to substrate binding and catalysis in the saccharopine dehydrogenase reaction

about

P2860

P2860

Contribution of K99 and D319 to substrate binding and catalysis in the saccharopine dehydrogenase reaction

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932