ライフサイエンスコーパス: adenylosuccinate

1 of AMP, coupling L-aspartate and IMP to form adenylosuccinate.

2 cated close to the succinyl moiety of docked adenylosuccinate.

3 d an apparent Km of approximately 24 mum for adenylosuccinate.

4 ndence of V(max) but no loss in affinity for adenylosuccinate.

5 hate, and Mg(2+), adopts the binding mode of adenylosuccinate.

6 s as an analogue of IMP or as an analogue of adenylosuccinate.

7 talytic acids in the subsequent formation of adenylosuccinate.

8 Within this pathway, the bifunctional enzyme adenylosuccinate (ADS) lyase plays a role in the formati

9 lude that 6-BDB-TAMP functions as a reactive adenylosuccinate analog in modifying His141 in the subst

10 lude that 6-BDB-TAMP functions as a reactive adenylosuccinate analogue in modifying both Arg131 and A

11 s of the purine nucleotide cycle (PNC): IMP, adenylosuccinate, and AMP.

12 rvations suggest that 2-BDB-TAMP attacks the adenylosuccinate binding site.

13 Adenylosuccinate binding studies of the other mutants re

14 rvations suggest that 6-BDB-TAMP targets the adenylosuccinate-binding site.

15 DP.Mg(2+).sulfate, the first structure of an adenylosuccinate-bound synthetase, reveals significant g

16 is subject to feedback inhibition by AMP and adenylosuccinate, but crystallographic complexes of the

17 ent of the reversible binding of radioactive adenylosuccinate by inactive mutant enzymes with substit

18 showed lower nucleotide synthesis on day 1: adenylosuccinate concentrations were 0.08 (0.04-0.12) re

19 d to a specific activity of 1.56 micromol of adenylosuccinate converted/min/mg protein for wild-type

20 Adenylosuccinate forms from 6-phosphoryl-IMP and l-aspar

21 rom GTP and IMP followed by the formation of adenylosuccinate from 6-phosphoryl-IMP and l-aspartate.

22 tase, putatively catalyzing the formation of adenylosuccinate from an intermediate of 6-phosphoryl-IM

23 The complex of adenylosuccinate.GDP.Mg(2+).sulfate, the first structure

24 AMP + 5 mM fumarate (the natural products of adenylosuccinate hydrolysis) but not by 0.1 mM 5'-AMP al

25 P is a competitive inhibitor with respect to adenylosuccinate in the catalytic reaction and also decr

26 an be explained by selective accumulation of adenylosuccinate in the Deltaasl knock-out and consequen

27 In H89Q, the K(M) for adenylosuccinate increases slightly to 2.5-fold that of

28 The K(m) for adenylosuccinate is elevated in the X62D mutants, and I6

29 6E are considerably reduced and affinity for adenylosuccinate is retained.

30 Adenylosuccinate lyase (ADSL) deficiency is a rare autos

31 Human adenylosuccinate lyase (ASL) deficiency is an inherited

32 Both adenylosuccinate synthetase (ADSS) and adenylosuccinate lyase (ASL) have been identified as vit

33 Tetrameric adenylosuccinate lyase (ASL) of Bacillus subtilis cataly

34 Adenylosuccinate lyase (ASL) of Bacillus subtilis is a h

35 Adenylosuccinate lyase (ASL), a catalyst of key reaction

36 ygous for two mutations in the gene encoding adenylosuccinate lyase (ASL), resulting in the protein m

37 ase (hpt), adenylosuccinate synthase (purA), adenylosuccinate lyase (purB), auxiliary protein (nrdI),

38 tetramer and this structure is essential for adenylosuccinate lyase activity.

39 d Arg(301) are indispensable to catalysis by adenylosuccinate lyase and probably interact noncovalent

40 ate sites in adenylosuccinate synthetase and adenylosuccinate lyase and to regulatory sites of glutam

41 Thus 2-BDB-TAMP reacts with adenylosuccinate lyase at a site distinct from the His14

42 studies suggest that 2-BDB-TAMP inactivates adenylosuccinate lyase by specific reaction at the subst

43 Adenylosuccinate lyase catalyzes two separate reactions

44 show here for the first time that wild-type adenylosuccinate lyase exhibits a protein concentration

45 In adenylosuccinate lyase from Bacillus subtilis, Gln(212),

46 Surprisingly, the structure of adenylosuccinate lyase from P. aerophilum reveals that t

47 The crystal structure of adenylosuccinate lyase from the hyperthermophilic archae

48 re of the tetrameric assembly are similar to adenylosuccinate lyase from the thermophilic eubacterium

49 Thus, adenylosuccinate lyase has four active sites per enzyme

50 d not inhibit adenylosuccinate synthetase or adenylosuccinate lyase isolated from Zea mays.

51 esidue Glu275 (both His141 and Glu275 are in adenylosuccinate lyase numbering), acts as the general b

52 Adenylosuccinate lyase of Bacillus subtilis is a tetrame

53 Adenylosuccinate lyase of Bacillus subtilis is inactivat

54 Adenylosuccinate lyase of Bacillus subtilis is inactivat

55 Through its dual action in this pathway, adenylosuccinate lyase plays an integral part in cellula

56 Rabbit muscle adenylosuccinate lyase upon incubation with 7.5-50 muM 2

57 A tetrameric structure of adenylosuccinate lyase was constructed by homology model

58 Asn(276) of Bacillus subtilis adenylosuccinate lyase, a residue corresponding to the l

59 Adenylosuccinate lyase, an enzyme catalyzing two reactio

60 kinase, anaerobic ribonucleotide reductase, adenylosuccinate lyase, and a hypothetical protein.

61 he de novo purine biosynthesis pathway, ASL (adenylosuccinate lyase, Step 8) and ATIC (5-aminoimidazo

62 ying His141 in the substrate-binding site of adenylosuccinate lyase, where it may serve as a general

63 the substrate binding site of rabbit muscle adenylosuccinate lyase.

64 nt for the catalytic activity of B. subtilis adenylosuccinate lyase.

65 41 is the reaction product of 6-BDB-TAMP and adenylosuccinate lyase.

66 Mutant adenylosuccinate lyases of Bacillus subtilis were prepar

67 position 276 result in structurally impaired adenylosuccinate lyases which are assembled into defecti

68 -4(N-succinylocarboxamide)ribonucleotide and adenylosuccinate, optimizing their bound orientations.

69 incorporation of [32P]reagent is provided by adenylosuccinate or a combination of AMP and fumarate, w

70 Active site nucleotides, either adenylosuccinate or IMP + GTP, prevent both slower phase

71 Active-site ligands, either adenylosuccinate or IMP and GTP, completely prevent inac

72 purine biosynthesis (the cleavage of either adenylosuccinate or succinylaminoimidazole carboxamide r

73 Adenylosuccinate, or a combination of AMP and fumarate,

74 Binding studies using [2-3H]-adenylosuccinate reveal that none of the Glu275 mutant e

75 ) in human erythrocytes or recombinant human adenylosuccinate synthase (ADSS).

76 ine-guanine phosphoribosyltransferase (hpt), adenylosuccinate synthase (purA), adenylosuccinate lyase

77 Both adenylosuccinate synthetase (ADSS) and adenylosuccinate

78 Adenylosuccinate synthetase (AdSS) is the site of action

79 carnitine palmitoyl transferase I and muscle adenylosuccinate synthetase (ADSS1).

80 A muscle-specific isoform of adenylosuccinate synthetase (AdSS1, EC) is one of three

81 tered activity of the IMP utilizing enzymes, adenylosuccinate synthetase (PurA) and IMP dehydrogenase

82 e reported that 1.9 kilobase pairs of murine adenylosuccinate synthetase 1 gene (Adss1) 5'-flanking D

83 otide analogs directed to substrate sites in adenylosuccinate synthetase and adenylosuccinate lyase a

84 The activities of IMPDH, adenylosuccinate synthetase and GMP reductase were two t

85 Wild-type adenylosuccinate synthetase and three mutant synthetases

86 site of action of hydantocidin and establish adenylosuccinate synthetase as an herbicide target of co

87 nalysis of the mode of inhibition of a plant adenylosuccinate synthetase by the active metabolite 5'-

88 Adenylosuccinate synthetase catalyzes the first committe

89 eriments, that suggest that Escherichia coli adenylosuccinate synthetase contains two shared active s

90 sults indicate that both subunits of dimeric adenylosuccinate synthetase contribute to each active si

91 of the stringent response, potently inhibits adenylosuccinate synthetase from Escherichia coli as an

92 Crystal structures of adenylosuccinate synthetase from Escherichia coli comple

93 Structures of adenylosuccinate synthetase from Escherichia coli comple

94 mplete set of substrate/substrate analogs of adenylosuccinate synthetase from Escherichia coli induce

95 The state of aggregation of adenylosuccinate synthetase from Escherichia coli is a p

96 Adenylosuccinate synthetase from Escherichia coli is ina

97 Adenylosuccinate synthetase from Escherichia coli is ina

98 A crystal structure of adenylosuccinate synthetase from Escherichia coli, compl

99 re not involved in the chemical mechanism of adenylosuccinate synthetase from Escherichia coli, yet t

100 ytic function and structural organization of adenylosuccinate synthetase from Escherichia coli.

101 Crystal structures of adenylosuccinate synthetase from Esherichia coli complex

102 es containing a synthetic promoter/antisense adenylosuccinate synthetase gene.

103 Adenylosuccinate synthetase governs the committed step o

104 Adenylosuccinate synthetase governs the first committed

105 including EF-Tu, Ypt1, rab-5, and FtsY, and adenylosuccinate synthetase have been reported to bind x

106 Hydantocidin itself did not inhibit adenylosuccinate synthetase or adenylosuccinate lyase is

107 ion was alluded to by use of mutant forms of adenylosuccinate synthetase previously prepared by site-

108 ure and site-directed mutagenesis of E. coli adenylosuccinate synthetase show that Arg303 interacts w

109 Prokaryotes have a single form of adenylosuccinate synthetase that controls the committed

110 IMP to XMP or AMP (IMP dehydrogenase, guaB; adenylosuccinate synthetase, purA, and ADE12), and unabl

111 Asp13 and His41 are essential residues of adenylosuccinate synthetase, putatively catalyzing the f

112 ertebrates have acidic and basic isozymes of adenylosuccinate synthetase, which participate in the fi

113 sponding positions in all known sequences of adenylosuccinate synthetase.

114 for SAICAR synthetase that parallels that of adenylosuccinate synthetase.

115 from IMP because of a developmental loss of adenylosuccinate synthetase.

116 tructure determination of a basic isozyme of adenylosuccinate synthetase.

117 Vertebrates possess two isozymes of adenylosuccinate synthetase.

118 both Arg131 and Arg303 in the active site of adenylosuccinate synthetase.

119 in the crystal structure of Escherichia coli adenylosuccinate synthetase.

120 rved differences in ligand recognition among adenylosuccinate synthetases may be due in part to confo

121 V(max) for conversion of adenylosuccinate to AMP and fumarate is 0.57 micromol/mi

122 meric enzyme which catalyzes the cleavage of adenylosuccinate to AMP and fumarate.

123 novo synthesis of IMP, and the conversion of adenylosuccinate to AMP, which occurs in the de novo syn

124 Bacillus subtilis catalyzes the cleavage of adenylosuccinate to form AMP and fumarate.