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1 by catalyzing incorporation of its cofactor, pyridoxal phosphate.
2 do not form heterotetramers, and do not bind pyridoxal phosphate.
3 e pyrroline ring with the aldehyde carbon of pyridoxal phosphate.
4 nting stable formation of a Schiff base with pyridoxal phosphate.
5 idue interacts with the pyridine nitrogen of pyridoxal phosphate.
6 s form external aldimines with the coenzyme, pyridoxal phosphate.
7 The enzyme contains covalently bound pyridoxal phosphate.
8 to stabilize the 3'O- functionality of bound pyridoxal phosphate.
9 ition about 8 angstrom from the phosphate of pyridoxal phosphate.
10 nd the nonselective P2 receptor antagonists, pyridoxal phosphate 6-azophenyl-2',4'-disulfonic acid an
11 rents were blocked by 100 microm suramin and pyridoxal phosphate 6-azophenyl-2',4'-disulfonic acid.
12 The P2Y receptor antagonists suramin and pyridoxal phosphate 6-azophenyl-2'-4'-disulfonic acid bo
14 ythroidine and reduced by the P2X antagonist pyridoxal phosphate-6-azo (benzene-2,4-disulfonic acid (
15 r ATP, and by blocking P2 purinoceptors with pyridoxal phosphate-6-azo(benzene-2,4-disulfonic acid) t
17 ts were potentiated by low concentrations of pyridoxal phosphate-6-azophenyl-2', 4'-disulfonic acid a
19 osine-3', 5'-bisphosphate (K(i)=900 nM), and pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid (K
20 ramin (100 micromol/L) or the P2X antagonist pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid (P
21 as blunted after the P2X receptor antagonist pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid (P
22 ed in low divalent cation medium, blocked by pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid (P
23 e) inhibition by Brilliant Blue G, Cu2+, and pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid te
24 (1 microM), but persisted in the presence of pyridoxal phosphate-6-azophenyl-2',4'-disulphonic acid (
25 ion of the P2 purinergic receptor antagonist pyridoxal phosphate-6-azophenyl-2',4'-disulphonic acid (
26 5-na phthalene-trisulphonic acid) and PPADS (pyridoxal phosphate-6-azophenyl-2',4'-disulphonic acid).
29 eptor antagonists periodate-oxidized ATP and pyridoxal-phosphate-6-azophenyl-2', 4'-disulfonic acid,
30 adult rats show that bilateral injections of pyridoxal-phosphate-6-azophenyl-2',4'-disulfonate (PPADS
31 blocked by P2Y receptor antagonists suramin, pyridoxal-phosphate-6-azophenyl-2',4'-disulfonate (PPADS
33 s with the broad-spectrum antagonists PPADS (pyridoxal-phosphate-6-azophenyl-2',4'-disulfonate) or RB
34 by the antagonists suramin (300 microM) and pyridoxal-phosphate-6-azophenyl-2',4'-disulfonic acid (3
35 e sensitivity to the antagonists suramin and pyridoxal-phosphate-6-azophenyl-2',4'-disulfonic acid (P
36 d by a pyridoxal-phosphate-based antagonist (pyridoxal-phosphate-6-azophenyl-2',4'-disulfonic acid) o
37 was blocked by the P(2) receptor antagonist pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
38 P2 receptor antagonists suramin (0.02 M) and pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
39 by 97 +/- 2% by the P2X receptor antagonist, pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
40 blocked by the broad P2 receptor antagonist pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
41 blocked by the broad P2 receptor antagonist pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
42 ed to MA; (iii) the P2X receptor antagonist, pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
43 yrrhetinic acid, blocking ATP receptors with pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
45 e or no effect on sensitivity to suramin and pyridoxal-phosphate-6-azophenyl-2,4-disulfonate in chime
46 r, which is inhibited by NF449, suramin, and pyridoxal-phosphate-6-azophenyl-2,4-disulfonate, with re
47 ), which forms an internal aldimine with the pyridoxal phosphate and catalyzes the abstraction of the
49 a-His(86) plays a structural role in binding pyridoxal phosphate and in stabilizing the correct orien
53 s of very slow biological reactions, notably pyridoxal phosphate and the ceric ion, are shown to meet
54 ny chromogenic cofactor, and the presence of pyridoxal phosphate and the mechanistically related pyru
55 interaction of His(86) with the phosphate of pyridoxal phosphate and with Lys(87) lowers the pK(a) of
56 Unexpectedly, the double bond linking the pyridoxal-phosphate and benzoate moieties was reduced by
58 en fasting plasma levels of vitamin B(6), as pyridoxal phosphate, and subsequent myocardial infarctio
59 xygen-sensitive and biotin-, ATP-, thiamin-, pyridoxal phosphate-, and metal-ion-independent, reversi
63 hould be measured, and therapeutic trials of pyridoxal phosphate as well as pyridoxine should be cons
64 The protein contained a highly conserved pyridoxal phosphate attachment site in the C-terminal do
66 LPS-induced iNOS expression is mimicked by a pyridoxal-phosphate-based antagonist (pyridoxal-phosphat
67 isomal aggregation (Gly41Arg), inhibition of pyridoxal phosphate binding and loss of catalytic activi
68 cement of His(86) by leucine (H86L) weakened pyridoxal phosphate binding approximately 20-fold and ab
69 DhpH is a multidomain protein, in which a pyridoxal phosphate binding domain is fused to an N-acet
71 at several key residues directly involved in pyridoxal phosphate binding were strictly conserved.
73 o acid sequence of CGS1 contains a consensus pyridoxal phosphate-binding site and is similar to MetB
76 studies of the enzyme because the different pyridoxal phosphate-bound intermediates can be followed
77 lyzes the second step in the biosynthesis of pyridoxal phosphate by oxidizing 4-phospho-d-erythronate
78 tational study of nonenzymatic and enzymatic pyridoxal phosphate-catalyzed decarboxylation of 2-amino
79 ne forms a stable external aldimine with the pyridoxal phosphate coenzyme at the active site of the b
80 tated by the spectroscopic properties of the pyridoxal phosphate coenzyme that forms a series of inte
82 e provides information on the binding of the pyridoxal phosphate cofactor as well as on amino acid re
84 ases via reactions of the compounds with the pyridoxal phosphate cofactor forming an irreversible add
85 interacts with the pyridine nitrogen of the pyridoxal phosphate cofactor from a neutral Ser (beta-Se
87 ing strain of E. coli and shown to contain a pyridoxal phosphate cofactor, as judged by ultraviolet/v
88 s328 is positioned greater than 17A from the pyridoxal phosphate cofactor, suggesting that a large co
92 A of the glycine alpha-carbon of the glycine-pyridoxal phosphate complex; the complex appears to be p
94 Residual activity of K165M is insensitive to pyridoxal phosphate, confirming K165 as the target of th
98 NIFS protein from Azobacter vinelandii is a pyridoxal phosphate-containing homodimer that catalyzes
99 e enzyme binds the substrate cysteine in the pyridoxal phosphate-containing site, and a persulfide is
100 rnal aldimine form of NtdA with the cofactor pyridoxal phosphate covalently attached to Lys-247.
102 ucose-6-phosphate 3-dehydrogenase, NtdA is a pyridoxal phosphate-dependent 3-oxo-glucose-6-phosphate:
103 ylacetaldehyde (4-HPAA), Rhodiola contains a pyridoxal phosphate-dependent 4-HPAA synthase that direc
104 at the primary amino acid level with several pyridoxal phosphate-dependent amino acid decarboxylases.
106 ine beta-synthase found in yeast catalyzes a pyridoxal phosphate-dependent condensation of homocystei
109 nzymological source of the amine moiety as a pyridoxal phosphate-dependent decarboxylating enzyme tha
110 uted cysteine desulfurase that catalyzes the pyridoxal phosphate-dependent desulfuration of L-cystein
112 The catalytic effects of perdeuterating the pyridoxal phosphate-dependent enzyme alanine racemase fr
113 S. cerevisiae FKF had been reported to be a pyridoxal phosphate-dependent enzyme encoded by BNA3.
114 Cystathionine gamma-synthase (CGS) is a pyridoxal phosphate-dependent enzyme that catalyzes a ga
115 oxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent enzyme that catalyzes the
116 Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate-dependent enzyme that catalyzes the
118 e aminotransferase (GABA-AT) is a tetrameric pyridoxal phosphate-dependent enzyme that catalyzes tran
123 a sugar aminotransferase that catalyzes the pyridoxal phosphate-dependent equatorial transamination
125 vivo and in vitro enzyme assays, supports a pyridoxal phosphate-dependent mechanism of Sec-tRNA(Sec)
127 erature, and of isotopic substitution on the pyridoxal phosphate-dependent reaction of L-serine with
131 Among them, we identified the L136 gene as a pyridoxal phosphate-dependent sugar aminotransferase.
132 e and that AGXT2L1 and AGXT2L2 catalyzed the pyridoxal-phosphate-dependent breakdown of phosphoethano
134 three-gene operon that potentially encodes a pyridoxal-phosphate-dependent enzyme, an extracellular s
135 1 and AGXT2L2, two closely related, putative pyridoxal-phosphate-dependent enzymes encoded by vertebr
137 homogeneous enzyme were characteristic of a pyridoxal phosphate enzyme and showed the absence of hem
138 (EC 2.1.2.1), a member of the alpha-class of pyridoxal phosphate enzymes, catalyzes the reversible in
139 which belong to two different fold types of pyridoxal phosphate enzymes: an aspartate aminotransfera
140 anistic studies showed that the enzyme-bound pyridoxal phosphate forms a Schiff's base with the amino
142 plants, the pathway for de novo synthesis of pyridoxal phosphate has been well characterized, however
145 nd in stabilizing the correct orientation of pyridoxal phosphate in the active site of the beta subun
146 t the active site lysine that normally binds pyridoxal phosphate in the cSHMT protein is exposed to s
147 nd to interact with the pyridine nitrogen of pyridoxal phosphate in the structure of alanine racemase
148 imelate epimerase is a representative of the pyridoxal phosphate-independent amino acid racemases, fo
149 To study the physiological role of Ala AT, a pyridoxal phosphate inhibitor, aminooxyacetic acid, was
154 y X-rays to create a covalent linkage of the pyridoxal-phosphate moiety to lysine 120 in the binding
155 se is a unique heme protein that catalyzes a pyridoxal phosphate (or PLP)-dependent beta-replacement
156 ositions Thr313 for its interaction with the pyridoxal phosphate oxygens and substrate alpha-carboxyl
158 ervation that the active form of vitamin B6 (pyridoxal phosphate, P5P) modulates the self-assembly of
160 e vitamin B-6 vitamer composition of plasma [pyridoxal phosphate (PLP) > pyridoxic acid (PA) > pyrido
161 olated and recombinant enzymes are devoid of pyridoxal phosphate (PLP) and are rapidly inactivated up
165 transaminase is a bacterial enzyme that uses pyridoxal phosphate (PLP) as a cofactor to catalyze the
171 ve been determined crystallographically: the pyridoxal phosphate (PLP) form and a complex with the re
172 ridoxal 5'-phosphate and failure to maintain pyridoxal phosphate (PLP) levels results in epilepsy.
173 enzyme that requires the cofactors heme and pyridoxal phosphate (PLP) to catalyze the condensation o
174 their cofactors (the pterins and vitamin B6 (pyridoxal phosphate (PLP))) in human cerebrospinal fluid
176 CAS and the Gm-CAS K95A mutant with a linked pyridoxal phosphate (PLP)-Cys molecule in the active sit
177 a-synthase is a hemeprotein that catalyzes a pyridoxal phosphate (PLP)-dependent condensation of seri
179 nzyme is a unique hemeprotein that catalyzes pyridoxal phosphate (PLP)-dependent condensation of seri
181 t: (i) the bioinformatics analysis reveals a pyridoxal phosphate (PLP)-dependent domain, we termed cy
182 n to be a mechanism-based inactivator of the pyridoxal phosphate (PLP)-dependent enzyme gamma-aminobu
183 xymethyltransferase (cSHMT) is a tetrameric, pyridoxal phosphate (PLP)-dependent enzyme that catalyze
184 lglycine decarboxylase (DGD) is a tetrameric pyridoxal phosphate (PLP)-dependent enzyme that catalyze
185 to the recent report that E. coli BioB is a pyridoxal phosphate (PLP)-dependent enzyme with intrinsi
189 l therapies for inherited diseases involving pyridoxal phosphate (PLP)-dependent enzymes, including p
190 ase (PanD), the enzyme in M. jannaschii is a pyridoxal phosphate (PLP)-dependent l-aspartate decarbox
191 onic acid (DAPA) synthase (EC 2.6.1.62) is a pyridoxal phosphate (PLP)-dependent transaminase that ca
195 l of homocysteine in mammals begins with the pyridoxal phosphate- (PLP-) dependent beta-replacement r
198 hildren with intractable seizures respond to pyridoxal phosphate rather than pyridoxine, including a
199 bilizing the protonated pyridine nitrogen of pyridoxal phosphate, reducing the pKa of the internal al
200 and formation of the external aldimine with pyridoxal phosphate required for early steps in SufS cat
201 optimum, Km values, and the requirement for pyridoxal phosphate resemble those of bacterial racemase
203 two enzymes of the biosynthetic pathway for pyridoxal phosphate (SerC and PdxA), we have found that
204 kinase (PRK) is inactivated upon exposure to pyridoxal phosphate/sodium borohydride, suggesting a rea
205 ues 1-353) is catalytically active and binds pyridoxal phosphate stoichiometrically establishes that
206 concentrations of glutamate or the cofactor pyridoxal phosphate, suggesting a noncompetitive inhibit
207 te kinetic parameters including the K(d) for pyridoxal phosphate, suggesting that the C-terminal resi
208 lyzed by this enzyme suggests a role for the pyridoxal phosphate, the role of the heme is uncertain.
209 lly thought to be due to abnormal binding of pyridoxal phosphate to glutamic acid decarboxylase resul
210 referred to as Pat) that, in the presence of pyridoxal phosphate, transfers the primary amino group o
214 5'-phosphate as the product, indicated that pyridoxal phosphate was not directly involved in the rea
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