Kutzneria sp. 744 ornithine N-hydroxylase, KtzI-FADox-Br

NIAID Data Ecosystem2026-05-01 收录

酶催化机制

微生物代谢工程

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Kutzneria sp. 744 ornithine N-hydroxylase, KtzI-FADox-Br

创建时间：

2023-09-27

How important are entropic contributions to enzyme catalysis?

酶催化机制

熵效应计算模拟

The idea that enzymes accelerate their reactions by entropic effects has played a major role in many prominent proposals about the origin of enzyme catalysis. This idea implies that the binding to an

PubMed Central2000-10-24 更新10

Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae

蛋白质晶体学

酶催化机制

Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae

NIAID Data Ecosystem00

Crystal structure of cofactor-free urate oxidase in complex with its 5-peroxoisourate intermediate (X-ray dose, 2.2 kGy)

结构生物学

酶催化机制

Crystal structure of cofactor-free urate oxidase in complex with its 5-peroxoisourate intermediate (X-ray dose, 2.2 kGy)

NIAID Data Ecosystem00

Cryo-EM Structure of Sf9 produced recombinant N-acetyltransferase 10 (NAT10) in complex with cytidine-amide-CoA bisubstrate probe and ADP/Mg2+.

蛋白质结构解析

酶催化机制

Cryo-EM Structure of Sf9 produced recombinant N-acetyltransferase 10 (NAT10) in complex with cytidine-amide-CoA bisubstrate probe and ADP/Mg2+.

NIAID Data Ecosystem00

CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE

酶催化机制

蛋白质晶体学

CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE

NIAID Data Ecosystem00

Kutzneria sp. 744 ornithine N-hydroxylase, KtzI-FADox-Br

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