Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate

Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate

Item
http://www.wikidata.org/entity/Q27640353
From Genome to Structure and Back Again: A Family Portrait of the TranscarbamylasesStructure of the catalytic trimer ofMethanococcus jannaschiiaspartate transcarbamoylase in an orthorhombic crystal formStructure of theAeropyrum pernixL7Ae multifunctional protein and insight into its extreme thermostabilityStructure of the catalytic chain ofMethanococcus jannaschiiaspartate transcarbamoylase in a hexagonal crystal form: insights into the path of carbamoyl phosphate to the active site of the enzymeDetecting coevolution in and among protein domainsStructure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis.Multisubstrate adduct inhibitors: drug design and biological tools.Crystallization and preliminary X-ray analysis of aspartate transcarbamoylase from the parasitic protist Trypanosoma cruzi.New experimental approaches for investigating interactions between Pyrococcus furiosus carbamate kinase and carbamoyltransferases, enzymes involved in the channeling of thermolabile carbamoyl phosphate.The extraordinary thermal stability of EstA from S. islandicus is independent of post translational modifications.Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum.Exploring the structural features of Aspartate Trans Carbamoylase (TtATCase) from Thermus thermophilus HB8 through in silico approaches: a potential drug target for inborn error of pyrimidine metabolism.
P2860

Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate

Item
http://www.wikidata.org/entity/Q27640353
description
2003 nî lūn-bûn
@nan
2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի փետրվարին հրատարակված գիտական հոդված
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2003年の論文
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2003年論文
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2003年論文
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2003年論文
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2003年論文
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2003年論文
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2003年论文
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name
Aspartate transcarbamylase fro ...... e N-phosphonacetyl-L-aspartate
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Aspartate transcarbamylase fro ...... e N-phosphonacetyl-L-aspartate
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Aspartate transcarbamylase fro ...... e N-phosphonacetyl-L-aspartate
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type
label
Aspartate transcarbamylase fro ...... e N-phosphonacetyl-L-aspartate
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Aspartate transcarbamylase fro ...... e N-phosphonacetyl-L-aspartate
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Aspartate transcarbamylase fro ...... e N-phosphonacetyl-L-aspartate
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Aspartate transcarbamylase fro ...... e N-phosphonacetyl-L-aspartate
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Aspartate transcarbamylase fro ...... e N-phosphonacetyl-L-aspartate
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Aspartate transcarbamylase fro ...... e N-phosphonacetyl-L-aspartate
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Aspartate transcarbamylase fro ...... e N-phosphonacetyl-L-aspartate
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10.1016/S0022-2836(02)01228-7
P407
P433
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P698
P921