ArticleThe Biochemical journal1997
Recombinant expression and isolation of human L-arginine:glycine amidinotransferase and identification of its active-site cysteine residue.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 35 citations in OpenAlex.
- Gliomas phenocopy an inborn error of metabolism to drive neuronal activity and tumor growth.Cell · 2026Article
- ClinGen variant curation expert panel recommendations for classification of variants in GAMT, GATM and SLC6A8 for cerebral creatine deficiency syndromes.Molecular genetics and metabolism · 2024Article
- Substrate Promiscuity of a Paralytic Shellfish Toxin Amidinotransferase.ACS chemical biology · 2020Article
- Characterization of Aphanizomenon ovalisporum amidinotransferase involved in cylindrospermopsin synthesis.MicrobiologyOpen · 2013Article
- Cysteine 351 is an essential nucleophile in catalysis by Porphyromonas gingivalis peptidylarginine deiminase.Archives of biochemistry and biophysics · 2010Article
- Automatic prediction of catalytic residues by modeling residue structural neighborhood.BMC bioinformatics · 2010Article
- Phytochelatin synthase, papain's cousin, in stereo.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Weeds, worms, and more. Papain's long-lost cousin, phytochelatin synthase.Plant physiology · 2004Review
- Arginine:glycine amidinotransferase deficiency: the third inborn error of creatine metabolism in humans.American journal of human genetics · 2001Article
- Op18/stathmin caps a kinked protofilament-like tubulin tetramer.The EMBO journal · 2000Article
- Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis.The EMBO journal · 1997Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Creatine and its phosphorylated form play a central role in the energy metabolism of muscle and nerve tissues. l-Arginine:glycine amidinotransferase (AT) catalyses the committed step in the formation of creatine. The mitochondrial and cytosolic forms of the enzyme are believed to derive from the same gene by alternative splicing. We have expressed recombinant human AT in Escherichia coli with two different N-termini, resembling the longest two forms of the enzyme that we had isolated recently from porcine kidney mitochondria as a mixture. The enzymes were expressed with N-terminal histidine tags followed by factor Xa-cleavage sites. We established a new method for the removal of N-terminal fusion peptides by means of an immobilized snake venom prothrombin activator. We identified cysteine-407 as the active-site residue of AT by radioactive labelling and isolation of labelled peptides, and by site-directed mutagenesis of the protein.
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