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1 do not form heterotetramers, and do not bind pyridoxal phosphate.
2 e pyrroline ring with the aldehyde carbon of pyridoxal phosphate.
3 nting stable formation of a Schiff base with pyridoxal phosphate.
4 by catalyzing incorporation of its cofactor, 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 of aldolases whose activity is dependent on pyridoxal phosphate.
11 nd the nonselective P2 receptor antagonists, pyridoxal phosphate 6-azophenyl-2',4'-disulfonic acid an
12 rents were blocked by 100 microm suramin and pyridoxal phosphate 6-azophenyl-2',4'-disulfonic acid.
13 The P2Y receptor antagonists suramin and pyridoxal phosphate 6-azophenyl-2'-4'-disulfonic acid bo
15 ythroidine and reduced by the P2X antagonist pyridoxal phosphate-6-azo (benzene-2,4-disulfonic acid (
16 r ATP, and by blocking P2 purinoceptors with pyridoxal phosphate-6-azo(benzene-2,4-disulfonic acid) t
18 ts were potentiated by low concentrations of pyridoxal phosphate-6-azophenyl-2', 4'-disulfonic acid a
20 osine-3', 5'-bisphosphate (K(i)=900 nM), and pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid (K
21 ed in low divalent cation medium, blocked by pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid (P
22 ramin (100 micromol/L) or the P2X antagonist pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid (P
23 as blunted after the P2X receptor antagonist pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid (P
24 e) inhibition by Brilliant Blue G, Cu2+, and pyridoxal phosphate-6-azophenyl-2',4'-disulfonic acid te
25 (1 microM), but persisted in the presence of pyridoxal phosphate-6-azophenyl-2',4'-disulphonic acid (
26 ion of the P2 purinergic receptor antagonist pyridoxal phosphate-6-azophenyl-2',4'-disulphonic acid (
27 5-na phthalene-trisulphonic acid) and PPADS (pyridoxal phosphate-6-azophenyl-2',4'-disulphonic acid).
30 eptor antagonists periodate-oxidized ATP and pyridoxal-phosphate-6-azophenyl-2', 4'-disulfonic acid,
31 adult rats show that bilateral injections of pyridoxal-phosphate-6-azophenyl-2',4'-disulfonate (PPADS
32 blocked by P2Y receptor antagonists suramin, pyridoxal-phosphate-6-azophenyl-2',4'-disulfonate (PPADS
34 s with the broad-spectrum antagonists PPADS (pyridoxal-phosphate-6-azophenyl-2',4'-disulfonate) or RB
35 by the antagonists suramin (300 microM) and pyridoxal-phosphate-6-azophenyl-2',4'-disulfonic acid (3
36 e sensitivity to the antagonists suramin and pyridoxal-phosphate-6-azophenyl-2',4'-disulfonic acid (P
37 d by a pyridoxal-phosphate-based antagonist (pyridoxal-phosphate-6-azophenyl-2',4'-disulfonic acid) o
38 was blocked by the P(2) receptor antagonist pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
39 P2 receptor antagonists suramin (0.02 M) and pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
40 by 97 +/- 2% by the P2X 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 blocked by the broad P2 receptor antagonist pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
43 ed to MA; (iii) the P2X receptor antagonist, pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
44 yrrhetinic acid, blocking ATP receptors with pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid (
46 e or no effect on sensitivity to suramin and pyridoxal-phosphate-6-azophenyl-2,4-disulfonate in chime
47 r, which is inhibited by NF449, suramin, and pyridoxal-phosphate-6-azophenyl-2,4-disulfonate, with re
48 ), which forms an internal aldimine with the pyridoxal phosphate and catalyzes the abstraction of the
50 a-His(86) plays a structural role in binding pyridoxal phosphate and in stabilizing the correct orien
54 s of very slow biological reactions, notably pyridoxal phosphate and the ceric ion, are shown to meet
55 ny chromogenic cofactor, and the presence of pyridoxal phosphate and the mechanistically related pyru
56 interaction of His(86) with the phosphate of pyridoxal phosphate and with Lys(87) lowers the pK(a) of
57 Unexpectedly, the double bond linking the pyridoxal-phosphate and benzoate moieties was reduced by
59 en fasting plasma levels of vitamin B(6), as pyridoxal phosphate, and subsequent myocardial infarctio
60 xygen-sensitive and biotin-, ATP-, thiamin-, pyridoxal phosphate-, and metal-ion-independent, reversi
64 hould be measured, and therapeutic trials of pyridoxal phosphate as well as pyridoxine should be cons
65 The protein contained a highly conserved pyridoxal phosphate attachment site in the C-terminal do
67 LPS-induced iNOS expression is mimicked by a pyridoxal-phosphate-based antagonist (pyridoxal-phosphat
68 isomal aggregation (Gly41Arg), inhibition of pyridoxal phosphate binding and loss of catalytic activi
69 cement of His(86) by leucine (H86L) weakened pyridoxal phosphate binding approximately 20-fold and ab
70 DhpH is a multidomain protein, in which a pyridoxal phosphate binding domain is fused to an N-acet
72 at several key residues directly involved in pyridoxal phosphate binding were strictly conserved.
73 CBS is a modular protein with a heme and pyridoxal phosphate-binding catalytic core, which is sep
75 for in vitro growth, and encodes a putative pyridoxal phosphate-binding protein of unknown function.
76 o acid sequence of CGS1 contains a consensus pyridoxal phosphate-binding site and is similar to MetB
79 studies of the enzyme because the different pyridoxal phosphate-bound intermediates can be followed
80 lyzes the second step in the biosynthesis of pyridoxal phosphate by oxidizing 4-phospho-d-erythronate
81 tational study of nonenzymatic and enzymatic pyridoxal phosphate-catalyzed decarboxylation of 2-amino
82 aldolase activity is an intrinsic feature of pyridoxal phosphate chemistry and identifies principles
83 ne forms a stable external aldimine with the pyridoxal phosphate coenzyme at the active site of the b
84 tated by the spectroscopic properties of the pyridoxal phosphate coenzyme that forms a series of inte
86 e provides information on the binding of the pyridoxal phosphate cofactor as well as on amino acid re
88 ases via reactions of the compounds with the pyridoxal phosphate cofactor forming an irreversible add
89 interacts with the pyridine nitrogen of the pyridoxal phosphate cofactor from a neutral Ser (beta-Se
91 ing strain of E. coli and shown to contain a pyridoxal phosphate cofactor, as judged by ultraviolet/v
92 s328 is positioned greater than 17A from the pyridoxal phosphate cofactor, suggesting that a large co
96 A of the glycine alpha-carbon of the glycine-pyridoxal phosphate complex; the complex appears to be p
98 Residual activity of K165M is insensitive to pyridoxal phosphate, confirming K165 as the target of th
102 NIFS protein from Azobacter vinelandii is a pyridoxal phosphate-containing homodimer that catalyzes
103 e enzyme binds the substrate cysteine in the pyridoxal phosphate-containing site, and a persulfide is
104 rnal aldimine form of NtdA with the cofactor pyridoxal phosphate covalently attached to Lys-247.
107 ucose-6-phosphate 3-dehydrogenase, NtdA is a pyridoxal phosphate-dependent 3-oxo-glucose-6-phosphate:
108 ylacetaldehyde (4-HPAA), Rhodiola contains a pyridoxal phosphate-dependent 4-HPAA synthase that direc
109 at the primary amino acid level with several pyridoxal phosphate-dependent amino acid decarboxylases.
111 ine beta-synthase found in yeast catalyzes a pyridoxal phosphate-dependent condensation of homocystei
114 nzymological source of the amine moiety as a pyridoxal phosphate-dependent decarboxylating enzyme tha
115 uted cysteine desulfurase that catalyzes the pyridoxal phosphate-dependent desulfuration of L-cystein
117 The catalytic effects of perdeuterating the pyridoxal phosphate-dependent enzyme alanine racemase fr
118 osynthesis of L-beta-ethynylserine where the pyridoxal phosphate-dependent enzyme BesB forms a rare t
119 S. cerevisiae FKF had been reported to be a pyridoxal phosphate-dependent enzyme encoded by BNA3.
120 Cystathionine gamma-synthase (CGS) is a pyridoxal phosphate-dependent enzyme that catalyzes a ga
122 oxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent enzyme that catalyzes the
123 Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate-dependent enzyme that catalyzes the
124 e aminotransferase (GABA-AT) is a tetrameric pyridoxal phosphate-dependent enzyme that catalyzes tran
129 understanding of the catalytic repertoire of pyridoxal phosphate-dependent enzymes and will enable de
131 a sugar aminotransferase that catalyzes the pyridoxal phosphate-dependent equatorial transamination
132 s study reassigns MilM as an oxygen (O(2))-, pyridoxal phosphate-dependent hydroxylase that hydroxyla
134 vivo and in vitro enzyme assays, supports a pyridoxal phosphate-dependent mechanism of Sec-tRNA(Sec)
136 erature, and of isotopic substitution on the pyridoxal phosphate-dependent reaction of L-serine with
140 Among them, we identified the L136 gene as a pyridoxal phosphate-dependent sugar aminotransferase.
141 c acid aminotransferase (BioA) catalyses the pyridoxal phosphate-dependent transamination of 7-keto-8
144 e and that AGXT2L1 and AGXT2L2 catalyzed the pyridoxal-phosphate-dependent breakdown of phosphoethano
146 three-gene operon that potentially encodes a pyridoxal-phosphate-dependent enzyme, an extracellular s
147 1 and AGXT2L2, two closely related, putative pyridoxal-phosphate-dependent enzymes encoded by vertebr
149 homogeneous enzyme were characteristic of a pyridoxal phosphate enzyme and showed the absence of hem
150 (EC 2.1.2.1), a member of the alpha-class of pyridoxal phosphate enzymes, catalyzes the reversible in
151 which belong to two different fold types of pyridoxal phosphate enzymes: an aspartate aminotransfera
152 anistic studies showed that the enzyme-bound pyridoxal phosphate forms a Schiff's base with the amino
154 plants, the pathway for de novo synthesis of pyridoxal phosphate has been well characterized, however
157 nd in stabilizing the correct orientation of pyridoxal phosphate in the active site of the beta subun
158 t the active site lysine that normally binds pyridoxal phosphate in the cSHMT protein is exposed to s
159 nd to interact with the pyridine nitrogen of pyridoxal phosphate in the structure of alanine racemase
160 imelate epimerase is a representative of the pyridoxal phosphate-independent amino acid racemases, fo
161 To study the physiological role of Ala AT, a pyridoxal phosphate inhibitor, aminooxyacetic acid, was
166 y X-rays to create a covalent linkage of the pyridoxal-phosphate moiety to lysine 120 in the binding
167 se is a unique heme protein that catalyzes a pyridoxal phosphate (or PLP)-dependent beta-replacement
168 ositions Thr313 for its interaction with the pyridoxal phosphate oxygens and substrate alpha-carboxyl
170 ervation that the active form of vitamin B6 (pyridoxal phosphate, P5P) modulates the self-assembly of
172 e vitamin B-6 vitamer composition of plasma [pyridoxal phosphate (PLP) > pyridoxic acid (PA) > pyrido
173 olated and recombinant enzymes are devoid of pyridoxal phosphate (PLP) and are rapidly inactivated up
177 structures reveal that covalent adducts with pyridoxal phosphate (PLP) are formed in the active site
178 transaminase is a bacterial enzyme that uses pyridoxal phosphate (PLP) as a cofactor to catalyze the
185 ysts represented the key to enable efficient pyridoxal phosphate (PLP) enzyme-catalyzed radical react
188 oxygen is activated by the organic cofactor pyridoxal phosphate (PLP) for oxidation reactions remain
189 ve been determined crystallographically: the pyridoxal phosphate (PLP) form and a complex with the re
190 and identified PDXK-an enzyme that produces pyridoxal phosphate (PLP) from vitamin B6-as an acute my
191 ridoxal 5'-phosphate and failure to maintain pyridoxal phosphate (PLP) levels results in epilepsy.
192 enzyme that requires the cofactors heme and pyridoxal phosphate (PLP) to catalyze the condensation o
193 f its active site histidine and lysine-bound pyridoxal phosphate (PLP) to the thiamin pyrimidine (HMP
194 their cofactors (the pterins and vitamin B6 (pyridoxal phosphate (PLP))) in human cerebrospinal fluid
196 CAS and the Gm-CAS K95A mutant with a linked pyridoxal phosphate (PLP)-Cys molecule in the active sit
197 a-synthase is a hemeprotein that catalyzes a pyridoxal phosphate (PLP)-dependent condensation of seri
199 nzyme is a unique hemeprotein that catalyzes pyridoxal phosphate (PLP)-dependent condensation of seri
201 t: (i) the bioinformatics analysis reveals a pyridoxal phosphate (PLP)-dependent domain, we termed cy
202 n to be a mechanism-based inactivator of the pyridoxal phosphate (PLP)-dependent enzyme gamma-aminobu
203 xymethyltransferase (cSHMT) is a tetrameric, pyridoxal phosphate (PLP)-dependent enzyme that catalyze
204 lglycine decarboxylase (DGD) is a tetrameric pyridoxal phosphate (PLP)-dependent enzyme that catalyze
205 to the recent report that E. coli BioB is a pyridoxal phosphate (PLP)-dependent enzyme with intrinsi
210 l therapies for inherited diseases involving pyridoxal phosphate (PLP)-dependent enzymes, including p
212 ase (PanD), the enzyme in M. jannaschii is a pyridoxal phosphate (PLP)-dependent l-aspartate decarbox
213 onic acid (DAPA) synthase (EC 2.6.1.62) is a pyridoxal phosphate (PLP)-dependent transaminase that ca
217 l of homocysteine in mammals begins with the pyridoxal phosphate- (PLP-) dependent beta-replacement r
220 hildren with intractable seizures respond to pyridoxal phosphate rather than pyridoxine, including a
221 bilizing the protonated pyridine nitrogen of pyridoxal phosphate, reducing the pKa of the internal al
222 and formation of the external aldimine with pyridoxal phosphate required for early steps in SufS cat
223 optimum, Km values, and the requirement for pyridoxal phosphate resemble those of bacterial racemase
225 two enzymes of the biosynthetic pathway for pyridoxal phosphate (SerC and PdxA), we have found that
226 kinase (PRK) is inactivated upon exposure to pyridoxal phosphate/sodium borohydride, suggesting a rea
227 ues 1-353) is catalytically active and binds pyridoxal phosphate stoichiometrically establishes that
228 concentrations of glutamate or the cofactor pyridoxal phosphate, suggesting a noncompetitive inhibit
229 te kinetic parameters including the K(d) for pyridoxal phosphate, suggesting that the C-terminal resi
230 was recently found to bind the cofactor PLP (pyridoxal phosphate, the active form of vitamin B(6)).
231 lyzed by this enzyme suggests a role for the pyridoxal phosphate, the role of the heme is uncertain.
232 del containing a pyridoxal-5'-phosphate (P5P/pyridoxal phosphate/the active form of vitamin B(6)) lig
233 lly thought to be due to abnormal binding of pyridoxal phosphate to glutamic acid decarboxylase resul
234 referred to as Pat) that, in the presence of pyridoxal phosphate, transfers the primary amino group o
238 5'-phosphate as the product, indicated that pyridoxal phosphate was not directly involved in the rea