(Q27748787)

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Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase

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Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase (English)

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T Nakatsu

1

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H Kato

series ordinal

2

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J Oda

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3

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publication date

January 1998

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published in

Nature structural biology

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volume

5

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page(s)

15-9

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issue

1

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Aspartyl-tRNA synthetase of the hyperthermophilic archaeon Pyrococcus sp. KOD1 has a chimerical structure of eukaryotic and bacterial enzymes.

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Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous

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Eleven down and nine to go.

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Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp)

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Structure and evolution of a group of related aminoacyl-tRNA synthetases

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7 January 2021

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Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase

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