From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

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2015 nî lūn-bûn

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2015 թուականին հրատարակուած գիտական յօդուած

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2015 թվականին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

@ast

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

@en

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

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type

Item

label

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

@ast

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

@en

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

@nl

prefLabel

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

@ast

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

@en

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

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P1476

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

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P2093

Mendel Tuchman

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Norma M Allewell

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Structural characterization of the enzymes composing the arginine deiminase pathway in Mycoplasma penetrans

Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD

Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.

Investigations into viomycin biosynthesis by using heterologous production in Streptomyces lividans

Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit

Integrated allosteric regulation in the S. cerevisiae carbamylphosphate synthetase - aspartate transcarbamylase multifunctional protein

Retrieving sequences of enzymes experimentally characterized but erroneously annotated : the case of the putrescine carbamoyltransferase

Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A

Mechanism of inactivation of ornithine transcarbamoylase by Ndelta -(N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism

Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation

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Dashuang Shi

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2015-08-12T00:00:00Z

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