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1 uccinyl-CoA to form CoA, carbon dioxide, and 5-aminolevulinate.
2 ant that forms a quinonoid intermediate with 5-aminolevulinate.
3 intermediate in the presence of the product, 5-aminolevulinate.
4 e A to yield coenzyme A, carbon dioxide, and 5-aminolevulinate.
5 of a quinonoid intermediate upon binding of 5-aminolevulinate.
6 yl-CoA and glycine are condensed to generate 5-aminolevulinate (ALA) by a dedicated PLP-dependent ALA
7 ehyde (GSA), 4,5-diaminovalerate (DAVA), and 5-aminolevulinate (ALA) indicated various transient chro
11 ions and protein fluorescence quenching upon 5-aminolevulinate binding demonstrated that the protein
14 inyl-CoA to produce carbon dioxide, CoA, and 5-aminolevulinate, in a reaction cycle involving the mec
15 f reaction of 5-aminolevulinate with ALAS is 5-aminolevulinate-independent, suggesting that it also r
16 ggest that turnover is limited by release of 5-aminolevulinate or a conformational change associated
17 rain, which can only grow in the presence of 5-aminolevulinate or when it is transformed with an acti
18 ally, the carbonyl and carboxylate groups of 5-aminolevulinate play a major protein-interacting role
20 is similar to that formed in the presence of 5-aminolevulinate, suggesting that release of this produ
21 the X chromosomal gene ALAS2, which encodes 5'-aminolevulinate synthase 2, in the affected females.
29 imiting enzyme in hepatic heme biosynthesis, 5-aminolevulinate synthase (ALAS-1), is regulated by the
31 -of-function mutations in erythroid-specific 5-aminolevulinate synthase (ALAS2), and new and experime
36 g enzymes of heme synthesis and degradation (5-aminolevulinate synthase 1 and heme oxygenase 1, respe
38 ns in the intron 1 GATA site (int-1-GATA) of 5-aminolevulinate synthase 2 (ALAS2) have been identifie
39 results provide conclusive evidence that the 5-aminolevulinate synthase active site is located at the
40 l increased hepatic nonheme iron and hepatic 5-aminolevulinate synthase activity in Hfe(-/-) but not
48 stopped-flow experiments of murine erythroid 5-aminolevulinate synthase demonstrate that reaction wit
49 es demonstrated that circular permutation of 5-aminolevulinate synthase does not prevent folding of t
50 able activity as determined using a standard 5-aminolevulinate synthase enzyme-coupled activity assay
51 ate or when it is transformed with an active 5-aminolevulinate synthase expression plasmid, the hem A
52 Lysine 313 (K313) of mature murine erythroid 5-aminolevulinate synthase forms a Schiff base linkage t
53 nolevulinic acid dehydratase (Alad), but not 5-aminolevulinate synthase gene (Alas2) or porphobilinog
56 d enhancers (HS-40 plus GATA-1 or HS-40 plus 5-aminolevulinate synthase intron 8 [I8] enhancers) and
57 esponding to the Arg-439 of murine erythroid 5-aminolevulinate synthase is a conserved residue in thi
59 y suggest that the conserved glycine loop in 5-aminolevulinate synthase is a pyridoxal 5'-phosphate c
61 sequencing of four Saccharomyces cerevisiae 5-aminolevulinate synthase mutants, which lack ALAS acti
63 cal and kinetic mechanisms and indicate that 5-aminolevulinate synthase operates under the stereoelec
64 gether, the data lead us to propose that the 5-aminolevulinate synthase overall structure can be reac
65 indicates that the natural continuity of the 5-aminolevulinate synthase polypeptide chain and the seq
66 is, much less is known about the role of the 5-aminolevulinate synthase polypeptide chain arrangement
68 ine 149, a conserved residue among all known 5-aminolevulinate synthase sequences, is essential for f
69 ional structure, active, circularly permuted 5-aminolevulinate synthase variants possess different to
70 f the polypeptide chain, circularly permuted 5-aminolevulinate synthase variants were constructed thr
71 ase, Arg-439 and Arg-433 of murine erythroid 5-aminolevulinate synthase were each replaced by Lys and
72 rrochelatase, porphobilinogen deaminase, and 5-aminolevulinate synthase) containing CACCC elements or
74 ved in substrate binding in murine erythroid 5-aminolevulinate synthase, Arg-439 and Arg-433 of murin
76 that in the active site of murine erythroid 5-aminolevulinate synthase, R439 is contributed from the
80 uinonoid intermediate formed upon binding of 5-aminolevulinate to the wild-type enzyme indicated that
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