The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

proC  -  pyrroline-5-carboxylate reductase

Escherichia coli UTI89

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of proC


High impact information on proC


Chemical compound and disease context of proC


Biological context of proC


Associations of proC with chemical compounds

  • We conclude that the proC gene is essential for symbiosis and suggest that the mutant does not obtain an exogenous supply of proline in association with soybeans sufficient to satisfy its auxotrophy [2].
  • Further, We showed that both LAT and pyrroline-5-carboxylate (P5C) reductase, the product of proC, were needed to convert L-Lys to L-PA in vitro [15].
  • The gene was cotransducible (Pl) with intermediate-level nitrofurantoin resistance and proC [16].
  • Analyses of a 12-mer and a 21-mer isolated from a cyanogen bromide digest were consistent with the proposition that the soybean P5CR isolated in these studies is very similar, although perhaps not identical, to the polypeptide predicted for the recently cloned soybean reductase (Delauney and Verma, 1990 Mol. Gen. Genet. 221, 299-305) [17].
  • Pyrroline-5-carboxylate reductase (P5CR) catalyzes the reduction of Delta1-pyrroline-5-carboxylate (P5C) to proline with concomitant oxidation of NAD(P)H to NAD(P)(+) [18].

Analytical, diagnostic and therapeutic context of proC


  1. Comparison of proC and other housekeeping genes of Pseudomonas aeruginosa with their counterparts in Escherichia coli. Savioz, A., Jeenes, D.J., Kocher, H.P., Haas, D. Gene (1990) [Pubmed]
  2. The Bradyrhizobium japonicum proline biosynthesis gene proC is essential for symbiosis. King, N.D., Hojnacki, D., O'Brian, M.R. Appl. Environ. Microbiol. (2000) [Pubmed]
  3. Molecular cloning and sequence analysis of the proC gene encoding delta 1-pyrroline-5-carboxylate reductase from an extremely thermophilic eubacterium Thermus thermophilus. Hoshino, T., Kosuge, T., Hidaka, Y., Tabata, K., Nakahara, T. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  4. Proline biosynthesis from L-ornithine in Clostridium sticklandii: purification of delta1-pyrroline-5-carboxylate reductase, and sequence and expression of the encoding gene, proC. Kenklies, J., Ziehn, R., Fritsche, K., Pich, A., Andreesen, J.R. Microbiology (Reading, Engl.) (1999) [Pubmed]
  5. Molecular organization of sbcC, a gene that affects genetic recombination and the viability of DNA palindromes in Escherichia coli K-12. Naom, I.S., Morton, S.J., Leach, D.R., Lloyd, R.G. Nucleic Acids Res. (1989) [Pubmed]
  6. Molecular cloning and evidence for osmoregulation of the delta 1-pyrroline-5-carboxylate reductase (proC) gene in pea (Pisum sativum L.). Williamson, C.L., Slocum, R.D. Plant Physiol. (1992) [Pubmed]
  7. Mapping by transposons of the inversion termini in Escherichia coli K-12 strain 1485IN. Enomoto, M., Komoda, Y., Tominaga, A. Genetics (1991) [Pubmed]
  8. Mutations in the Corynebacterium glutamicum proline biosynthetic pathway: a natural bypass of th proA step. Ankri, S., Serebrijski, I., Reyes, O., Leblon, G. J. Bacteriol. (1996) [Pubmed]
  9. Genetic and molecular analysis of aroL, the gene for shikimate kinase II in Escherichia coli K-12. DeFeyter, R.C., Pittard, J. J. Bacteriol. (1986) [Pubmed]
  10. Mapping of a new genetic locus responsible for ampicillin resistance in Escherichia coli. Buchanan, C.E., Strominger, J.L. J. Bacteriol. (1976) [Pubmed]
  11. Interaction of the expression of two membrane genes, acrA and plsA, in Escherichia coli K-12. Nakamura, H., Tojo, T., Greenberg, J. J. Bacteriol. (1975) [Pubmed]
  12. Isolation of unselected mutants of alkaline phosphatase in Escherichia coli through nitrosoguanidine comutation and comparison with natural variants. del Castillo, F., Cerdá-Olmedo, E. Biochem. Genet. (1984) [Pubmed]
  13. A soybean gene encoding delta 1-pyrroline-5-carboxylate reductase was isolated by functional complementation in Escherichia coli and is found to be osmoregulated. Delauney, A.J., Verma, D.P. Mol. Gen. Genet. (1990) [Pubmed]
  14. Possible involvement of a L-delta 1-pyrroline-5-carboxylate (P5C) reductase in the synthesis of proline in Desulfovibrio desulfuricans Norway. Fons, M., Cami, B., Chippaux, M. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  15. Biotransformation of L-lysine to L-pipecolic acid catalyzed by L-lysine 6-aminotransferase and pyrroline-5-carboxylate reductase. Fujii, T., Mukaihara, M., Agematu, H., Tsunekawa, H. Biosci. Biotechnol. Biochem. (2002) [Pubmed]
  16. The effects of chlorate- and streptomycin-resistance mutations on nitrofurantoin resistance in Escherichia coli K-12. Obaseiki-Ebor, E.E., Breeze, A.S. Can. J. Microbiol. (1984) [Pubmed]
  17. Pyrroline-5-carboxylate reductase in soybean nodules: isolation/partial primary structure/evidence for isozymes. Chilson, O.P., Kelly-Chilson, A.E., Siegel, N.R. Arch. Biochem. Biophys. (1991) [Pubmed]
  18. Purification, characterization, and crystallization of human pyrroline-5-carboxylate reductase. Meng, Z., Lou, Z., Liu, Z., Hui, D., Bartlam, M., Rao, Z. Protein Expr. Purif. (2006) [Pubmed]
  19. Purification and characterization of a functionally active Mycobacterium tuberculosis pyrroline-5-carboxylate reductase. Yang, Y., Xu, S., Zhang, M., Jin, R., Zhang, L., Bao, J., Wang, H. Protein Expr. Purif. (2006) [Pubmed]
  20. Electron microscopic heteroduplex studies of sequence relations among plasmids of Escherichia coli: structure of F13 and related F-primes. Hu, S., Ohtsubo, E., Davidson, N. J. Bacteriol. (1975) [Pubmed]
  21. Structure of genes and an insertion element in the methane producing archaebacterium Methanobrevibacter smithii. Hamilton, P.T., Reeve, J.N. Mol. Gen. Genet. (1985) [Pubmed]
WikiGenes - Universities