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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
8                                              5-Aminolevulinate (ALA), an essential metabolite in all
9 umulated high levels of hepatic URO when fed 5-aminolevulinate (ALA).
10 e and succinyl-CoA to generate CoA, CO2, and 5-aminolevulinate (ALA).
11 ions and protein fluorescence quenching upon 5-aminolevulinate binding demonstrated that the protein
12 n enol that is in rapid equilibrium with the 5-aminolevulinate-bound quinonoid species.
13  of glycine and succinyl coenzyme A produces 5-aminolevulinate, coenzyme A, and carbon dioxide.
14  first step in heme biosynthesis, generating 5'-aminolevulinate from glycine and succinyl-CoA.
15 inyl-CoA to produce carbon dioxide, CoA, and 5-aminolevulinate, in a reaction cycle involving the mec
16 f reaction of 5-aminolevulinate with ALAS is 5-aminolevulinate-independent, suggesting that it also r
17 ggest that turnover is limited by release of 5-aminolevulinate or a conformational change associated
18 rain, which can only grow in the presence of 5-aminolevulinate or when it is transformed with an acti
19 ally, the carbonyl and carboxylate groups of 5-aminolevulinate play a major protein-interacting role
20 e or a conformational change associated with 5-aminolevulinate release.
21 is similar to that formed in the presence of 5-aminolevulinate, suggesting that release of this produ
22                                              5'-aminolevulinate synthase (ALAS) catalyzes the first s
23 that hemoglobin-related transcripts (Hbb and 5'-aminolevulinate synthase 2 [Alas2]) increased 46-63%
24  the X chromosomal gene ALAS2, which encodes 5'-aminolevulinate synthase 2, in the affected females.
25  further increased the activities of hepatic 5-aminolevulinate synthase (ALAS) and CYP1A2.
26                                              5-Aminolevulinate synthase (ALAS) catalyzes the first st
27                                              5-Aminolevulinate synthase (ALAS) catalyzes the first st
28                                              5-Aminolevulinate synthase (ALAS) catalyzes the first st
29                                              5-Aminolevulinate synthase (ALAS) is the first enzyme of
30                                              5-Aminolevulinate synthase (ALAS), a pyridoxal 5'-phosph
31                                              5-Aminolevulinate synthase (ALAS), the first enzyme of t
32 imiting enzyme in hepatic heme biosynthesis, 5-aminolevulinate synthase (ALAS-1), is regulated by the
33                                    Erythroid 5-aminolevulinate synthase (ALAS-E) catalyzes the first
34 -of-function mutations in erythroid-specific 5-aminolevulinate synthase (ALAS2), and new and experime
35                                              5-Aminolevulinate synthase (EC 2.3.1.37) (ALAS), a pyrid
36                                              5-Aminolevulinate synthase (EC 2.3.1.37) catalyzes the f
37                                              5-Aminolevulinate synthase (EC 2.3.1.37) is the first en
38  the pyridoxal 5'-phosphate-dependent enzyme 5-aminolevulinate synthase (EC 2.3.1.37).
39 g enzymes of heme synthesis and degradation (5-aminolevulinate synthase 1 and heme oxygenase 1, respe
40                        Increased activity of 5-aminolevulinate synthase 2 (ALAS2) has been shown to a
41 ns in the intron 1 GATA site (int-1-GATA) of 5-aminolevulinate synthase 2 (ALAS2) have been identifie
42 gh substrate reduction therapy by inhibiting 5-aminolevulinate synthase 2 (ALAS2), the first and rate
43 results provide conclusive evidence that the 5-aminolevulinate synthase active site is located at the
44 l increased hepatic nonheme iron and hepatic 5-aminolevulinate synthase activity in Hfe(-/-) but not
45                                The wild-type 5-aminolevulinate synthase additionally forms a stable q
46           Homology sequence modeling between 5-aminolevulinate synthase and some other alpha-family p
47                       Although the wild type 5-aminolevulinate synthase and the circularly permuted v
48  quinonoid intermediate formation during the 5-aminolevulinate synthase catalytic cycle.
49                                              5-Aminolevulinate synthase catalyzes the condensation of
50                                              5-Aminolevulinate synthase catalyzes the first step of t
51                                              5-Aminolevulinate synthase catalyzes the pyridoxal 5'-ph
52 h pathway compartmentalization and improving 5-aminolevulinate synthase delivery by 1.62-fold and 4.7
53 stopped-flow experiments of murine erythroid 5-aminolevulinate synthase demonstrate that reaction wit
54 es demonstrated that circular permutation of 5-aminolevulinate synthase does not prevent folding of t
55 able activity as determined using a standard 5-aminolevulinate synthase enzyme-coupled activity assay
56 ate or when it is transformed with an active 5-aminolevulinate synthase expression plasmid, the hem A
57 Lysine 313 (K313) of mature murine erythroid 5-aminolevulinate synthase forms a Schiff base linkage t
58 nolevulinic acid dehydratase (Alad), but not 5-aminolevulinate synthase gene (Alas2) or porphobilinog
59 aused by mutations in the erythroid-specific 5-aminolevulinate synthase gene (ALAS2).
60 missense mutations in the erythroid-specific 5-aminolevulinate synthase gene (ALAS2).
61 d enhancers (HS-40 plus GATA-1 or HS-40 plus 5-aminolevulinate synthase intron 8 [I8] enhancers) and
62 esponding to the Arg-439 of murine erythroid 5-aminolevulinate synthase is a conserved residue in thi
63                                              5-Aminolevulinate synthase is a dimeric protein having a
64 y suggest that the conserved glycine loop in 5-aminolevulinate synthase is a pyridoxal 5'-phosphate c
65                                              5-Aminolevulinate synthase is the first enzyme of the he
66  sequencing of four Saccharomyces cerevisiae 5-aminolevulinate synthase mutants, which lack ALAS acti
67  site-directed, catalytically inactive mouse 5-aminolevulinate synthase mutants.
68 cal and kinetic mechanisms and indicate that 5-aminolevulinate synthase operates under the stereoelec
69 gether, the data lead us to propose that the 5-aminolevulinate synthase overall structure can be reac
70 indicates that the natural continuity of the 5-aminolevulinate synthase polypeptide chain and the seq
71 is, much less is known about the role of the 5-aminolevulinate synthase polypeptide chain arrangement
72 isplayed unique circular permutations of the 5-aminolevulinate synthase polypeptide chain.
73 ine 149, a conserved residue among all known 5-aminolevulinate synthase sequences, is essential for f
74 ional structure, active, circularly permuted 5-aminolevulinate synthase variants possess different to
75 f the polypeptide chain, circularly permuted 5-aminolevulinate synthase variants were constructed thr
76 ase, Arg-439 and Arg-433 of murine erythroid 5-aminolevulinate synthase were each replaced by Lys and
77 rrochelatase, porphobilinogen deaminase, and 5-aminolevulinate synthase) containing CACCC elements or
78 rrochelatase, porphobilinogen deaminase, and 5-aminolevulinate synthase).
79 ved in substrate binding in murine erythroid 5-aminolevulinate synthase, Arg-439 and Arg-433 of murin
80                           In mouse erythroid 5-aminolevulinate synthase, lysine 313 has been identifi
81  that in the active site of murine erythroid 5-aminolevulinate synthase, R439 is contributed from the
82 dependent condensation reaction catalyzed by 5-aminolevulinate synthase.
83 quences different from that of the wild type 5-aminolevulinate synthase.
84 ole in substrate binding of murine erythroid 5-aminolevulinate synthase.
85 uinonoid intermediate formed upon binding of 5-aminolevulinate to the wild-type enzyme indicated that
86                 The slow rate of reaction of 5-aminolevulinate with ALAS is 5-aminolevulinate-indepen
87                Reaction of either glycine or 5-aminolevulinate with ALAS is slow (kf = 0.15 s-1) and