Metabolism of Proline and of Hydroxyproline

Adams, Elijah

doi:10.1016/b978-0-12-363705-5.50007-5

Cited by 96 publications

(63 citation statements)

References 295 publications

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“…Proline and hydroxyproline are degraded by a series of analogous reactions (1). The biochemical similarity of these two degradative pathways suggests that the corresponding reactions in each pathway could be catalyzed by a common enzyme which can act on either substrate.…”

Section: Introductionmentioning

confidence: 99%

Genetic evidence for a common enzyme catalyzing the second step in the degradation of proline and hydroxyproline.

Valle¹,

Goodman²,

Harris³

et al. 1979

J. Clin. Invest.

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A B S T R A C T The initial step in the degradation pathways of proline and hydroxyproline is catalyzed by proline oxidase and hydroxyproline oxidase, yielding A1-pyrroline-5-carboxylate and A1-pyrroline-3-hydroxy-5-carboxylate, respectively. The second step is the oxidation of A1-pyrroline-5-carboxylate to glutamate and Al-pyrroline-3-hydroxy-5-carboxylate to y-hydroxyglutamate. To determine if this second step in the degradation of proline and hydroxyproline is catalyzed by a common or by separate enzyme(s), we developed a radioisotopic assay for Al-pyrroline-3-hydroxy-5-carboxylate dehydrogenase activity. We then compared Al-pyrroline-3-hydroxy-5-carboxylate dehydrogenase activity with that of Al-pyrroline-5-carboxylate dehydrogenase in fibroblasts and leukocytes from type II hyperprolinemia patients, heterozygotes, and controls. We found that cells from type II hyperprolinemia patients were deficient in both dehydrogenase activities. Furthermore, these activities were highly correlated over the range found in the normals, heterozygotes, and patients.We conclude from these data that a common Alpyrroline-5-carboxylate dehydrogenase catalyzes the oxidation of both Al-pyrroline-5-carboxylate and Alpyrroline-3-hydroxy-5-carboxylate, and that this activity is deficient in type II hyperprolinemia.

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Section: Introductionmentioning

confidence: 99%

Genetic evidence for a common enzyme catalyzing the second step in the degradation of proline and hydroxyproline.

Valle¹,

Goodman²,

Harris³

et al. 1979

J. Clin. Invest.

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“…In micro-organisms, proline is synthesized from glutamate via three enzymic reactions catalysed by y-glutamyl kinase (GK; proB product, EC 2.7.2.1 l), y-glutamyl phosphate reductase (GPR;proA product, EC 1.2.1.41) and 1 -pyrroline-5-carboxylate reductase (proC product, EC 1.5.1.2) (Adams & Frank, 1980). Feedback control mechanisms and genetic backgrounds for proline biosynthesis have been extensively studied in Escherichia coli K12.…”

Section: Introductionmentioning

confidence: 99%

Analysis of the Serratia marcescens proBA operon and feedback control of proline biosynthesis

Omori

Suzuki

Imai

et al. 1991

Journal of General Microbiology

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The proBA operon, coding for y-glutamyl b a s e (GK) and y-glutamyl phosphate reductase (GPR), was cloned from the chromosome of the wild-type strain of Serratia marcescens Sr41. From our sequence data the proB (1101 bp) and proA (1472 bp) genes were shown to code for two proteins of M, 39169 and 44640, respectively. Analysis of expression of the ZacZstructural gene fused with theproBA promoter showed that theproBA operon is not subject to proline-mediated feedback repression. Amplification of the proBA operon enabled us to determine GK activity, which was inhibited in the presence of a low concentration of L-proline. Comparison of the amino acid sequences of the S. marcescens GK and GPR proteins with those of the GI( and GPR proteins from E. coZi revealed extensive similarities.

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“…Pyrroline-5-carboxylate reductase (PCR) (EC 1.5.1.2), which catalyzes the final step in proline synthesis, converts pyrroline-5-carboxylic acid (PC) to proline in a NAD(P)H-dependent reaction (1,2). Although a number of studies have characterized the enzymes from bovine and rat liver (3)(4)(5), there have been few studies on PC reductase from normal human tissues.…”

Section: Introductionmentioning

confidence: 99%