| pubmed-article:7842857 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C0002563 | lld:lifeskim |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C0025831 | lld:lifeskim |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C0042092 | lld:lifeskim |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C2246401 | lld:lifeskim |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C1817482 | lld:lifeskim |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C1554080 | lld:lifeskim |
| pubmed-article:7842857 | lifeskim:mentions | umls-concept:C1706198 | lld:lifeskim |
| pubmed-article:7842857 | pubmed:dateCreated | 1995-3-9 | lld:pubmed |
| pubmed-article:7842857 | pubmed:abstractText | Two enzymes which play an important role in regulation and flux control through the tetapyrrole biosynthetic pathway are considered. The Rhodobacter sphaeroides 5-aminolaevulinic acid synthase isoenzymes are discussed and the progress being made on their recombinant expression and isolation is reported. The Escherichia coli uroporphyrinogen methylase, which is encoded by the cysG gene, is also examined. In this case evidence is provided which demonstrates that the gene product is responsible for the complete synthesis of sirohaem from uroporphyrinogen III. The enzyme is thus capable of performing two S-adenosylmethionine-dependent methylation reactions, an NADP(+)-dependent dehydrogenation and iron chelation. The uroporphyrinogen methylase is thus a small multifunctional enzyme. | lld:pubmed |
| pubmed-article:7842857 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7842857 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7842857 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7842857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7842857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7842857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7842857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7842857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7842857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7842857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7842857 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7842857 | pubmed:issn | 0300-5208 | lld:pubmed |
| pubmed-article:7842857 | pubmed:author | pubmed-author:BoleVV | lld:pubmed |
| pubmed-article:7842857 | pubmed:author | pubmed-author:WarrenM JMJ | lld:pubmed |
| pubmed-article:7842857 | pubmed:author | pubmed-author:WoodcockS CSC | lld:pubmed |
| pubmed-article:7842857 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7842857 | pubmed:volume | 180 | lld:pubmed |
| pubmed-article:7842857 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7842857 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7842857 | pubmed:pagination | 26-40; discussion 40-9 | lld:pubmed |
| pubmed-article:7842857 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:meshHeading | pubmed-meshheading:7842857-... | lld:pubmed |
| pubmed-article:7842857 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7842857 | pubmed:articleTitle | 5-Aminolaevulinic acid synthase and uroporphyrinogen methylase: two key control enzymes of tetrapyrrole biosynthesis and modification. | lld:pubmed |
| pubmed-article:7842857 | pubmed:affiliation | School of Biological Sciences, Queen Mary and Westfield College, University of London, UK. | lld:pubmed |
| pubmed-article:7842857 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7842857 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7842857 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7842857 | lld:pubmed |
