Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1

Pyrroline-5-carboxylate reductase (PYCR) is the final enzyme in proline biosynthesis, catalyzing the NAD(P)H-dependent reduction of Δ1-pyrroline-5-carboxylate (P5C) to proline. Mutations in the PYCR1 gene alter mitochondrial function and cause the connective tissue disorder cutis laxa. Furthermore,...

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Veröffentlicht in:	The Journal of biological chemistry 2017-04, Vol.292 (17), p.7233-7243
Hauptverfasser:	Christensen, Emily M., Patel, Sagar M., Korasick, David A., Campbell, Ashley C., Krause, Kurt L., Becker, Donald F., Tanner, John J.
Format:	Artikel
Sprache:	eng
Schlagworte:	analytical ultracentrifugation Binding Sites Catalytic Domain Crystallography, X-Ray delta-1-Pyrroline-5-Carboxylate Reductase enzyme kinetics Humans Kinetics Ligands Mutation NAD(P)H-dependent reductase NADP - chemistry nicotinamide adenine dinucleotide (NADH) Proline - chemistry Protein Binding Protein Multimerization Protein Structure and Folding Protein Structure, Quaternary Protein Structure, Tertiary Pyrroline Carboxylate Reductases - chemistry reductase Rossmann fold site-directed mutagenesis Substrate Specificity Ultracentrifugation X-ray crystallography
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