A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant.

G J Palm, J Lubkowski, Christian Derst (Co-author), S Schleper, K H Röhm, A Wlodawer

    Research output: Contribution to journalOriginal Articlepeer-review

    93 Citations (Web of Science)
    Original languageEnglish
    Pages (from-to)211-216
    JournalFEBS LETTERS
    Volume390
    Issue number2
    Publication statusPublished - 1996

    Keywords

    • GLUTAMINASE-ASPARAGINASE
    • SITE
    • BINDING
    • ACINETOBACTER
    • MUTAGENESIS
    • REFINEMENT
    • THREONINE

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