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Article

Transition state stabilization by six arginines clustered in the active site of creatine kinase.

Biochimica et biophysica acta - 10 Aug 2005

Jourden Michael J, Geiss Paul R, Thomenius Michael J, Horst Lindsay A, Barty Melissa M, Brym Melissa J, Mulligan Guy B, Almeida Ryan M, Kersteen Betsy A, Myers Nichole R, Snider Mark J, Borders Charles L, Edmiston Paul L

Abstract excerpt

Six fully conserved arginine residues (R129, R131, R235, R291, R319, and R340) closely grouped in the nucleotide binding site of rabbit muscle creatine kinase (rmCK) were mutated; four to alanine and all six to lysine. Kinetic analyses in the direction of phosphocreatine formation showed that all four alanine mutants led to substantial losses of activity with three (R129A, R131A, and R235A) having no detectable...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 16005271
DOI: 10.1016/j.bbapap.2005.06.002

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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