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1 AdoHcy competes with tracer in the antibody/tracer compl
2 AdoHcy hydrolase achieves catalysis of AdoHcy hydrolysis
3 AdoHcy hydrolase, which was inactivated with compound a,
4 AdoHcy is present in normal human plasma at concentratio
5 AdoHcy nucleosidase (EC 3.2.2.9) irreversibly cleaves Ad
6 s4-NH 2 + AdoMet --> p53-Lys4-N(Me)H 2 (+) + AdoHcy] in the SET7/9 complex is Delta G (++) = 20.1 +/-
7 -Lys4-NH 3 (+), SET7/9.p53-Lys4-N(Me)H 2 (+).AdoHcy, or SET7/9.p53-Lys4-N(Me)H 2 (+).AdoMet complex.
9 nsfer (Lys-N(Me)2 + AdoMet --> Lys-N(Me)3+ + AdoHcy) is associated with an allowed DeltaG++ of 25.9 +
10 n [Lys27-N(Me)2 + AdoMet --> Lys27-N(Me)3+ + AdoHcy] is associated with a DeltaG++ of 23.1 +/- 4.0 kc
11 riphosphate (ATP) by 5'-methylthio-adenosine/AdoHcy nucleosidase (MTAN), adenine phosphoribosyl trans
12 increase in hepatic S-adenosylhomocysteine (AdoHcy) (p < 0.01) concentrations, resulting in a 75% re
15 ersible inhibitor of S-adenosylhomocysteine (AdoHcy) hydrolase (EC 3.3.1.1), express increased AdoMet
17 Most inhibitors of S-adenosylhomocysteine (AdoHcy) hydrolase function as substrates for the "3'-oxi
19 rystal structures of S-adenosylhomocysteine (AdoHcy) hydrolase in the substrate-free, NAD(+) form and
20 potent inhibitors of S-adenosylhomocysteine (AdoHcy) hydrolase, we investigated the mechanisms by whi
23 hionine (AdoMet) and S-adenosylhomocysteine (AdoHcy) in plasma can be measured by formation of the fl
24 eine (Hcy) precursor S-adenosylhomocysteine (AdoHcy) may cause cellular hypomethylation in the settin
25 Accumulation of the S-adenosylhomocysteine (AdoHcy) product, a feedback inhibitor of TPMT, slows the
27 h methylated DNA and S-adenosylhomocysteine (AdoHcy) were obtained and evaluated as double-reciprocal
28 s designed to detect S-adenosylhomocysteine (AdoHcy), a product of all S-adenosylmethionine (AdoMet)-
31 cosine) and produces S-adenosylhomocysteine (AdoHcy), thereby controlling the methylating potential o
32 thylation reactions, S-adenosylhomocysteine (AdoHcy), which causes by-product inhibition of methyltra
39 uilibrium dissociation constants for AdoMet, AdoHcy and sinefungin were determined using an intrinsic
46 Hcy by AdoHcy nucleosidase, which alleviates AdoHcy product feedback inhibition of S-adenosylmethioni
49 introducing any major structural changes, an AdoHcy molecule can be placed in the catalytic domain.
50 The fluorescent derivatives of AdoMet and AdoHcy are then chromatographed by HPLC on a C-18 column
52 involves an initial separation of AdoMet and AdoHcy in deproteinized plasma by HPLC on a C-8 column f
55 A methyltransferases analogous to AdoMet and AdoHcy would affect the rate of enzyme-induced deaminati
59 t mice exhibited increased (>6-fold) Hcy and AdoHcy levels in all tissues examined compared with cont
60 resent severe accumulation of tissue Hcy and AdoHcy, protein arginine hypomethylation in liver and br
62 ence of AdoMet to C-24 methylated sterol and AdoHcy, was analyzed for amino acid residues that contri
67 Mock methyltransferase reactions using both AdoHcy and AdoMet indicated that the assay tolerated 1 t
68 ostatic potential originating from the bound AdoHcy extends to the DNA phosphate groups flanking the
71 f this assay is the destruction of AdoHcy by AdoHcy nucleosidase, which alleviates AdoHcy product fee
77 ss-linking to m7GpppA(pA)n was stimulated by AdoHcy, whereas cross-linking to GpppA(pA)n was unaffect
80 cleosidase (EC 3.2.2.9) irreversibly cleaves AdoHcy to adenine and S-ribosylhomocysteine, significant
82 hough the crystal structure does not contain AdoHcy or its analogue, there is a well-formed AdoHcy-bi
83 l studies of base flipping in the M.HhaI-DNA-AdoHcy ternary complex indicate that the south-constrain
85 The structures of the ternary protein/DNA/AdoHcy complexes for both the Glu119Ala and Glu119Gln mu
87 ailable anti-AdoHcy antibody and fluorescein-AdoHcy conjugate tracer to measure AdoHcy generated as a
89 A recently published rapid immunoassay for AdoHcy in human plasma should make measurement of this i
95 l transfer reaction (AdoMet + Lys-N(Me)H --> AdoHcy + Lys-N(Me)2H+) at the QM/MM level is 20.5 +/- 3.
96 transfer reaction [AdoMet + Lys27-N(Me)H --> AdoHcy + Lys27-N(Me)2H+] at the QM/MM level is 22.6 +/-
98 ET7/9 [Lys4-NH2 + AdoMet --> Lys4-N(Me)H2+ + AdoHcy] complex is DeltaG++ = 19.0 +/- 1.6 kcal/mol.
99 SET [Lys27-NH2 + AdoMet --> Lys27-N(Me)H2+ + AdoHcy] equals 22.5 +/- 4.3 kcal/mol, which is in excell
104 In this assay, S-adenosyl-l-homocysteine (AdoHcy or SAH), a common product of AdoMet-dependent tra
105 nd to the product S-adenosyl-L-homocysteine (AdoHcy) and magnesium, both with and without the natural
107 of the reaction, S-adenosyl-L-homocysteine (AdoHcy) and N,N-dimethyltryptamine, as well as antimigra
109 cofactor product S-adenosyl-l-homocysteine (AdoHcy) at 2.8 A resolution and identify a glutamate res
111 for binding with S-adenosyl-l-homocysteine (AdoHcy) hydrolase and/or addition of enzyme-bound water
113 Domain motions of S-adenosyl-l-homocysteine (AdoHcy) hydrolase have been detected by time-resolved fl
114 t inactivation of S-adenosyl-L-homocysteine (AdoHcy) hydrolase producing significant decreases in the
121 thyltransferases, S-adenosyl-L-homocysteine (AdoHcy) inhibited METTL7B activity in a competitive fash
122 cofactor product S-adenosyl-l-homocysteine (AdoHcy) provides the molecular basis for recognition of
125 Met), the product S-adenosyl-l-homocysteine (AdoHcy), the inhibitor sinefungin, as well as a mutant a
128 In this assay, S-adenosyl-L-homocysteine (AdoHcy/SAH), the transmethylation product of AdoMet-depe
130 In this assay, S-adenosyl-l-homocystine (AdoHcy/SAH), the by-product of PMT-involved methylation,
134 contrast, compound c completely inactivated AdoHcy hydrolase by converting 2 equiv of E-NAD(+) to E-
135 ssible mechanism by which BDDFHA inactivates AdoHcy hdyrolase is proposed: enzyme-mediated water addi
136 ese data suggest that compound c inactivates AdoHcy hydrolase by a mechanism similar to the acetyleni
137 ydro-5'-fluoroaristeromycin are inactivating AdoHcy hydrolase by directly reducing NAD+ to NADH and n
138 ional advantage of this assay which includes AdoHcy nucleosidase is the destruction of AdoHcy, thus a
139 eparture of the potentially potent inhibitor AdoHcy from the active site and thus facilitates the met
142 uorescein-AdoHcy conjugate tracer to measure AdoHcy generated as a result of methyltransferase activi
143 ntify the residues that bind the Hcy moiety, AdoHcy was docked to the closed form of AdoHcy hydrolase
148 udies) that a higher plasma concentration of AdoHcy is a more sensitive indicator of vascular disease
150 olases catalyze the reversible conversion of AdoHcy to adenosine and homocysteine, making use of a ca
151 dvantage of this assay is the destruction of AdoHcy by AdoHcy nucleosidase, which alleviates AdoHcy p
153 for the deprotonation after dissociation of AdoHcy (S-adenosyl-L-homocysteine) and before binding of
155 s been grown in the presence of an excess of AdoHcy, and its crystal structure has been determined at
158 olase catalyzes the reversible hydrolysis of AdoHcy to adenosine (Ado) and homocysteine (Hcy), playin
162 nt and concentration-dependent inhibition of AdoHcy hydrolase (K(i), 0.55 and 118.5 microM, respectiv
163 ndirect mechanism of DZNep via inhibition of AdoHcy-ase, once considered a liability due to possible
164 methylene)adenosine 2a, a known inhibitor of AdoHcy hydrolase not modified with a cyclopropyl ring at
165 potent type-I mechanism-based inhibitors of AdoHcy hydrolase with k2/Ki values of 4.4 x 10(6) and 8.
168 Higher levels of AdoMet and lower levels of AdoHcy were found in the brains of Pcmt1-/- mice, and to
169 l change so as to place the ribose moiety of AdoHcy in close proximity to the nicotinamide moiety of
170 of a redox partial reaction (3'-oxidation of AdoHcy at the beginning and 3'-reduction of Ado at the e
173 dro-5'-fluoraristeromycin in the presence of AdoHcy hydrolase did not release fluoride ion or generat
174 did cross-link to the cap in the presence of AdoHcy, suggesting that this mutation affects the chemic
178 ggests elements of the catalytic strategy of AdoHcy hydrolase for acceleration of the reversible conv
179 here do not exhibit an inhibitory effect on AdoHcy hydrolase and displayed only marginal antiviral a
180 otency for the inhibition of human placental AdoHcy hydrolase was: DZNep approximately NepA >> DZAri
182 both is a reason that measurement of plasma AdoHcy has not generally been carried out in large studi
183 Advantages of the measurement of plasma AdoHcy include 1) a smaller overlap of values between co
186 be used to assay other enzymes that produce AdoHcy, 5'-methylthioadenosine, or compounds that can be
188 AdoMet is inhibited by the reaction product AdoHcy (IC(50) 4 microm) and by substrate analogs sinefu
192 eactions, is first hydrolyzed by recombinant AdoHcy nucleosidase (EC 3.2.2.9) into adenine and S-ribo
195 attern of the catalytic domain suggests that AdoHcy molecules can travel freely to and from AdoHcyase
198 ations showed that binding of L-adenosine to AdoHcy hydrolase is weaker (higher energy) and less spec
200 ured for its quantitative linear response to AdoHcy and the ultrasensitivity to 0.3 pmol of AdoHcy.
201 However, 7b and 16b upon incubation with AdoHcy hydrolase were not metabolized suggesting that th