Phosphoglucomutase 3

Phosphoglucomutase 3

Phosphoglucomutase 3, also known as PGM3, is a human gene.cite web | title = Entrez Gene: PGM3 phosphoglucomutase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5238| accessdate = ]

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References

Further reading

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*cite journal | author=Chen SH, Anderson JE, Giblett ER, Stamatoyannopoulos G |title=Isozyme patterns in erythrocytes from human fetuses. |journal=Am. J. Hematol. |volume=3 |issue= |pages= 23–8 |year= 1978 |pmid= 203189 |doi=
*cite journal | author=Yoshida H, Abe T, Nakamura F |title=Studies on the frequencies of PGM1, PGM3 and Es-D types from hair roots in Japanese subjects and the determination of these types from old hair roots. |journal=Forensic Sci. Int. |volume=14 |issue= 1 |pages= 1–7 |year= 1979 |pmid= 468082 |doi=
*cite journal | author=Marshall MJ, Neal FE, Goldberg DM |title=Isoenzymes of hexokinase, 6-phosphogluconate dehydrogenase, phosphoglucomutase and lactate dehydrogenase in uterine cancer. |journal=Br. J. Cancer |volume=40 |issue= 3 |pages= 380–90 |year= 1980 |pmid= 508567 |doi=
*cite journal | author=Cantu JM, Ibarra B |title=Phosphoglucomutase: evidence for a new locus expressed in human milk. |journal=Science |volume=216 |issue= 4546 |pages= 639–40 |year= 1982 |pmid= 6461922 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Li C, Rodriguez M, Banerjee D |title=Cloning and characterization of complementary DNA encoding human N-acetylglucosamine-phosphate mutase protein. |journal=Gene |volume=242 |issue= 1-2 |pages= 97–103 |year= 2000 |pmid= 10721701 |doi=
*cite journal | author=Mio T, Yamada-Okabe T, Arisawa M, Yamada-Okabe H |title=Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis. |journal=Biochim. Biophys. Acta |volume=1492 |issue= 2-3 |pages= 369–76 |year= 2000 |pmid= 11004509 |doi=
*cite journal | author=Pang H, Koda Y, Soejima M, Kimura H |title=Identification of human phosphoglucomutase 3 (PGM3) as N-acetylglucosamine-phosphate mutase (AGM1). |journal=Ann. Hum. Genet. |volume=66 |issue= Pt 2 |pages= 139–44 |year= 2003 |pmid= 12174217 |doi= 10.1017/S0003480002001033
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Mungall AJ, Palmer SA, Sims SK, "et al." |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504

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  • Phosphoglucomutase — Masse/Länge Primärstruktur 561 Aminosäuren …   Deutsch Wikipedia

  • Phosphoglucomutase — (EC number|5.4.2.2) is an enzyme that transfers a phosphoryl group on a glucose monomer from the 1 to the 6 position in the forward direction or the 6 to the 1 position in the reverse.More specifically, it facilitates the interconversion of… …   Wikipedia

  • Phosphoglucomutase — La phosphoglucomutase est une enzyme de la glycogénogenèse qui catalyse la réaction : glucose 6 phosphate → glucose 1 phosphate Comme toutes les mutases, son action ne consiste qu à déplacer un groupement phosphate entre deux carbones d une… …   Wikipédia en Français

  • phosphoglucomutase — phosphoglucomutase. См. глюкозофосфомутаза. (Источник: «Англо русский толковый словарь генетических терминов». Арефьев В.А., Лисовенко Л.А., Москва: Изд во ВНИРО, 1995 г.) …   Молекулярная биология и генетика. Толковый словарь.

  • Phosphoglucomutase (glucose-cofactor) — In enzymology, a phosphoglucomutase (glucose cofactor) (EC number|5.4.2.5) is an enzyme that catalyzes the chemical reaction:alpha D glucose 1 phosphate ightleftharpoons D glucose 6 phosphateHence, this enzyme has one substrate, alpha D glucose 1 …   Wikipedia

  • phosphoglucomutase — noun Date: 1938 an enzyme found in all plant and animal cells that catalyzes the reversible isomerization of glucose 1 phosphate to glucose 6 phosphate …   New Collegiate Dictionary

  • phosphoglucomutase — noun Any enzyme that catalyzes the interconversion of isomers of glucose phosphates …   Wiktionary

  • phosphoglucomutase — An enzyme that catalyzes the reversible reaction, α d glucose 1 phosphate ⇋ α d glucose 6 phosphate, with glucose 1,6 bisphosphate a necessary cofactor; one of the steps in glycogenolysis. SYN: glucose phosphomutase. * * * phos·pho·glu·co·mu·tase …   Medical dictionary

  • phosphoglucomutase — (PGM)    Among the first genetically polymorphic enzymes to be studied by electrophoresis …   Forensic science glossary

  • phosphoglucomutase — phos·pho·glu·co·mutase …   English syllables

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