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1 CAIR binds to the free enzyme up to 200-fold more tightl
2 CAIR-1 sequence is identical, save 2 amino acids, to BAG
3 CAIR-1/BAG-3 contains several PXXP SH3 binding domains l
4 CAIR-1/BAG-3 forms an EGF-regulated ternary complex with
5 CAIR-1/BAG-3 from control and EGF-treated cell lysates b
6 CAIR-1/BAG-3 is phosphorylated in vivo in the absence of
8 Here we report the X-ray structures of N(5)-CAIR synthetase from Escherichia coli with either MgATP
10 ctural analysis of Aspergillus clavatus N(5)-CAIR synthetase solved in the presence of either Mg(2)AT
11 inoimidazole ribonucleotide synthetase (N(5)-CAIR synthetase) converts 5-aminoimidazole ribonucleotid
12 inoimidazole ribonucleotide synthetase (N(5)-CAIR synthetase), a key enzyme in microbial de novo puri
14 CAIR) by two enzymes: N(5)-carboxy-AIR (N(5)-CAIR) synthetase (PurK) and N(5)-CAIR mutase (class I Pu
19 troaminoimidazole ribonucleotide (NO2-AIR, a CAIR analogue) and structures of H45N and H45Q PurEs soa
21 D-ribofuranosyl)imidazole-4-carboxylic acid (CAIR) along a reaction sequence involving a tandem N-for
23 he crystal structures of the ADP and the ADP.CAIR complexes of SAICAR synthetase from Escherichia col
24 leotide (AIR) is converted to 4-carboxy-AIR (CAIR) by two enzymes: N(5)-carboxy-AIR (N(5)-CAIR) synth
25 azole ribonucleotide (AIR) to 4-carboxy-AIR (CAIR) represents an unusual divergence in purine biosynt
29 H3 interaction, PLC-gamma was pulled down by CAIR-1/BAG-3 PXXP-GST fusions, but GST-PXXP constructs c
30 nd 5-aminoimidazole-4-carboxyribonucleotide (CAIR) to 5-aminoimidazole-4-(N-succinylcarboxamide) ribo
32 nSO4 stopping reagent is proposed to chelate CAIR, enabling delayed analysis of this acid-labile prod
34 , buried carboxylate or CO2 binding site for CAIR and N5-CAIR in a hydrophobic pocket in which the ca
35 N5-CAIR is transferred directly to generate CAIR without equilibration with CO2/HCO3- in solution.
37 a mechanism for the purE-catalyzed N5-CAIR-->CAIR biosynthetic one that involves a carboxylative sp3-
38 of the inactive mutant H59N-AaPurE soaked in CAIR showed that protonation of CAIR C4 can occur in the
39 of a phosphoryl transfer reaction involving CAIR and ATP, but also supports an alternative chemical
40 engineered to overexpress either full-length CAIR-1 (FL), which binds Hsp70, or a BAG domain-deletion
41 er with a reasonable mechanism for the model CAIRs-->FAIRs synthetic transformation is interpreted to
42 echanism of this rearrangement, [4,7-13C]-N5-CAIR and [7-14C]-N5-CAIR were synthesized and separately
43 rrangement, [4,7-13C]-N5-CAIR and [7-14C]-N5-CAIR were synthesized and separately incubated with PurE
44 supported by DFT calculations on CAIR and N5-CAIR analogues in which the ribose 5'-phosphate is repla
45 boxylate or CO2 binding site for CAIR and N5-CAIR in a hydrophobic pocket in which the carboxylate or
46 upport a mechanism for the purE-catalyzed N5-CAIR-->CAIR biosynthetic one that involves a carboxylati
47 interconversion of acid-labile compounds N5-CAIR and 4-carboxy-5-aminoimidazole ribonucleotide (CAIR
49 boxyaminoimidazole ribonucleotide mutase (N5-CAIR mutase or PurE) from Escherichia coli catalyzes the
50 the carboxylate group of the carbamate of N5-CAIR is transferred directly to generate CAIR without eq
53 talyzes the reversible interconversion of N5-CAIR to carboxyaminoimidazole ribonucleotide (CAIR) with
54 N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) in a reaction that requires both ATP and HCO3-.
55 N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) mutase (PurE) catalyzes the reversible interconver
56 N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) synthetase, catalyzes the conversion of 5-aminoimi
57 bstrate for proton transfer from His45 to N5-CAIR to form an enzyme-bound aminoimidazole ribonucleoti
60 same oxygen atom of the 4-carboxyl group of CAIR; whereas, the third coordinates the alpha- and beta
63 ons suggest that the nonaromatic tautomer of CAIR (isoCAIR) is only 3.1 kcal/mol higher in energy tha
65 ransfers is supported by DFT calculations on CAIR and N5-CAIR analogues in which the ribose 5'-phosph
67 f 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) in the purine pathway in most prokaryotes requires
68 s 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) to 4-(N-succinylcarboxamide)-5-aminoimidazole ribo
72 stin proteasomal inhibition, indicating that CAIR-1 inhibits proteasomal degradation distal to protei
81 P is a competitive inhibitor with respect to CAIR, suggesting the possibility of a hydrogen bond inte
82 tructures of H45N and H45Q PurEs soaked with CAIR have been determined and provide the first insight
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