Crystal structure and mechanism of human L‐arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis
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Summary
The crystal structure of the recombinant human enzyme by multiple isomorphous replacement at 1.9 Å resolution is determined and a reaction mechanism with a catalytic triad Cys–His–Asp is proposed on the basis of substrate and product bound states.
- Type
- dissertation
- Published
- 1998-01-28
- Cited by
- 121
- References
- 49
- Access
- Open access
- OpenAlex
- https://openalex.org/W9218780
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:12433328
Keywords
Popular music, Art, Visual arts
References
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- Genèse des cibles des autoanticorps anti-protéines citrullinées dans le tissu synovial rhumatoïde : peptidyl-arginine désiminases et fibrine citrullinée
- Differential Gene Expression Profiling of Dystrophic Dog Muscle after MuStem Cell Transplantation
- Biosynthesis of homoarginine (hArg) and asymmetric dimethylarginine (ADMA) from acutely and chronically administered free l-arginine in humans
- Blood-CNS transport mechanisms in pathophysiology and drug delivery
- Getting past appearances: the many-fold consequences of remote homology
- Estrogen modulates the expression of L‐arginine:glycine amidinotransferase in chick liver
- Response to Paoli
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- The capacity for the de novo biosynthesis of creatine is present in the tunicate Ciona intestinalis and is likely widespread in other protochordate and invertebrate groups.
- Homoarginine Levels Are Regulated by L-Arginine: Glycine Amidinotransferase and Affect Stroke Outcome Results From Human and Murine Studies
- Substrate binding and catalysis by L-arginine:glycine amidinotransferase--a mutagenesis and crystallographic study.
- Cysteine 351 is an Essential Nucleophile in Catalysis by Porphyromonas gingivalis Peptidylarginine Deiminase
- A novel gene encoding amidinotransferase in the cylindrospermopsin producing cyanobacterium Aphanizomenon ovalisporum.