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1 A to yield coenzyme A, carbon dioxide, and 5-aminolevulinate.
2 f a quinonoid intermediate upon binding of 5-aminolevulinate.
3 cinyl-CoA to form CoA, carbon dioxide, and 5-aminolevulinate.
4 t that forms a quinonoid intermediate with 5-aminolevulinate.
5 termediate in the presence of the product, 5-aminolevulinate.
6 -CoA and glycine are condensed to generate 5-aminolevulinate (ALA) by a dedicated PLP-dependent ALA s
7 ession of the mammalian genes encoding delta-aminolevulinate (ALA) dehydratase and porphobilinogen de
8 yde (GSA), 4,5-diaminovalerate (DAVA), and 5-aminolevulinate (ALA) indicated various transient chromo
11 nsfectants, which gave the same phenotype of aminolevulinate (ALA)-inducible uroporphyria as found in
14 te clearance, with photodynamic therapy with aminolevulinate (ALA-PDT) showing the most favorable ris
15 li HB101 grown in LB medium containing delta-aminolevulinate and Fe(NO3)3 has a red color, while the
16 use of newer fluorescence agents (hexylester aminolevulinate and hypericin) and their application to
17 ns and protein fluorescence quenching upon 5-aminolevulinate binding demonstrated that the protein co
21 structure of the gene encoding murine delta-aminolevulinate dehydratase (ALAD; EC4.2.1.24), which is
23 d in this organism; however, an NADPH-linked aminolevulinate dehydrogenase activity was demonstrated.
26 observed that mutant cells were resistant to aminolevulinate-dependent toxicity, as expected if the h
28 of aminolevulinate synthase and diversion of aminolevulinate from the pathway by aminolevulinate dehy
30 d aminolevulinic acid hydrochloride ormethyl aminolevulinate hydrochloride as stabilizers with 10 or
31 pretreatment, followed by 3 hours of methyl aminolevulinate hydrochloride incubation and subsequent
32 yl-CoA to produce carbon dioxide, CoA, and 5-aminolevulinate, in a reaction cycle involving the mecha
33 reaction of 5-aminolevulinate with ALAS is 5-aminolevulinate-independent, suggesting that it also rep
34 iverged in the presence of either glycine or aminolevulinate, indicating that the reorientation of th
36 rophyll, suggesting that the majority of the aminolevulinate is diverted from the common tetrapyrrole
37 very low), photodynamic therapy with methyl aminolevulinate (MAL-PDT) (RR, 5.95; 95% CI, 1.21-29.41;
38 est that turnover is limited by release of 5-aminolevulinate or a conformational change associated wi
39 in, which can only grow in the presence of 5-aminolevulinate or when it is transformed with an active
40 uorouracil cream, 5% imiquimod cream, methyl aminolevulinate photodynamic therapy (MAL-PDT), or 0.015
42 ly, the carbonyl and carboxylate groups of 5-aminolevulinate play a major protein-interacting role by
43 glycine binding before succinyl-CoA and with aminolevulinate release after CoA and carbon dioxide.
45 similar to that formed in the presence of 5-aminolevulinate, suggesting that release of this product
54 tes heme biosynthesis by activation of delta-aminolevulinate synthase (ALAS), which catalyzes the fir
55 imiting enzyme of heme biosynthesis is delta-aminolevulinate synthase (ALAS), which is localized in m
56 iting enzyme in hepatic heme biosynthesis, 5-aminolevulinate synthase (ALAS-1), is regulated by the p
59 h promotes heme synthesis by activation of d-aminolevulinate synthase (ALAS/Hem1) in yeast and regula
60 f-function mutations in erythroid-specific 5-aminolevulinate synthase (ALAS2), and new and experiment
61 odes the erythroid-specific isoform of delta-aminolevulinate synthase (ALAS2; also known as ALAS-E),
66 ced stabilization of the mRNA encoding delta aminolevulinate synthase 1 (ALAS1), the rate-limiting en
68 enzymes of heme synthesis and degradation (5-aminolevulinate synthase 1 and heme oxygenase 1, respect
70 in the intron 1 GATA site (int-1-GATA) of 5-aminolevulinate synthase 2 (ALAS2) have been identified
71 substrate reduction therapy by inhibiting 5-aminolevulinate synthase 2 (ALAS2), the first and rate-l
72 t hemoglobin-related transcripts (Hbb and 5'-aminolevulinate synthase 2 [Alas2]) increased 46-63% in
73 e X chromosomal gene ALAS2, which encodes 5'-aminolevulinate synthase 2, in the affected females.
74 sults provide conclusive evidence that the 5-aminolevulinate synthase active site is located at the s
75 increased hepatic nonheme iron and hepatic 5-aminolevulinate synthase activity in Hfe(-/-) but not wi
78 d by a combination of feedback inhibition of aminolevulinate synthase and diversion of aminolevulinat
79 IREs encoded by erythroid heme biosynthetic aminolevulinate synthase and Hif-2alpha mRNAs, which pre
83 e proposal that D279 plays a crucial role in aminolevulinate synthase catalysis by enhancing the elec
88 pathway compartmentalization and improving 5-aminolevulinate synthase delivery by 1.62-fold and 4.76-
89 opped-flow experiments of murine erythroid 5-aminolevulinate synthase demonstrate that reaction with
90 demonstrated that circular permutation of 5-aminolevulinate synthase does not prevent folding of the
91 le activity as determined using a standard 5-aminolevulinate synthase enzyme-coupled activity assay.
92 e or when it is transformed with an active 5-aminolevulinate synthase expression plasmid, the hem A-
93 sine 313 (K313) of mature murine erythroid 5-aminolevulinate synthase forms a Schiff base linkage to
95 levulinic acid dehydratase (Alad), but not 5-aminolevulinate synthase gene (Alas2) or porphobilinogen
98 enhancers (HS-40 plus GATA-1 or HS-40 plus 5-aminolevulinate synthase intron 8 [I8] enhancers) and WP
99 ponding to the Arg-439 of murine erythroid 5-aminolevulinate synthase is a conserved residue in this
101 suggest that the conserved glycine loop in 5-aminolevulinate synthase is a pyridoxal 5'-phosphate cof
103 equencing of four Saccharomyces cerevisiae 5-aminolevulinate synthase mutants, which lack ALAS activi
105 l and kinetic mechanisms and indicate that 5-aminolevulinate synthase operates under the stereoelectr
107 ther, the data lead us to propose that the 5-aminolevulinate synthase overall structure can be reache
108 dicates that the natural continuity of the 5-aminolevulinate synthase polypeptide chain and the seque
109 , much less is known about the role of the 5-aminolevulinate synthase polypeptide chain arrangement i
111 e 149, a conserved residue among all known 5-aminolevulinate synthase sequences, is essential for fun
112 f the catalytic domain of all members of the aminolevulinate synthase superfamily of proteins of whic
113 nal structure, active, circularly permuted 5-aminolevulinate synthase variants possess different topo
114 the polypeptide chain, circularly permuted 5-aminolevulinate synthase variants were constructed throu
115 as increased approximately twofold and delta-aminolevulinate synthase was increased approximately 50%
116 e, Arg-439 and Arg-433 of murine erythroid 5-aminolevulinate synthase were each replaced by Lys and L
117 ochelatase, porphobilinogen deaminase, and 5-aminolevulinate synthase) containing CACCC elements or G
119 ncreases in the mRNAs of cytochrome c, delta-aminolevulinate synthase, and citrate synthase also occu
120 RNA) or a C-bulge (in m-aconitase, erythroid aminolevulinate synthase, and transferrin receptor mRNAs
121 d in substrate binding in murine erythroid 5-aminolevulinate synthase, Arg-439 and Arg-433 of murine
123 hat in the active site of murine erythroid 5-aminolevulinate synthase, R439 is contributed from the s
128 roid enzyme was found to be conserved in all aminolevulinate synthases and appeared to be homologous
130 nonoid intermediate formed upon binding of 5-aminolevulinate to the wild-type enzyme indicated that t
131 ated with non-AFXL (median, 2898 AU), methyl aminolevulinate-treated controls (median, 2254 AU), and
132 as demonstrated that less than 20% of [(14)C]aminolevulinate was incorporated into bacteriochlorophyl