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1 densation of serine and homocysteine to form cystathionine.
2 t condensation of serine and homocysteine to cystathionine.
3 eine, ribosylhomocysteine, homocysteine, and cystathionine.
4 densation of homocysteine and serine to form cystathionine.
5 on of l-serine with l-homocysteine to form l-cystathionine.
6 t condenses homocysteine with serine to form cystathionine.
7 74F substitution, allowing better access for cystathionine.
8 e cycle by the conversion of homocysteine to cystathionine.
9 lation or the appearance of homocysteine and cystathionine.
13 ysteine with serine or with cysteine to form cystathionine and either water or hydrogen sulfide, resp
14 S(Hp) mutant was restored by homocysteine or cystathionine and growth of the DeltacysK(Hp) mutant by
17 ensation of serine and homocysteine to yield cystathionine and is the single most common locus of mut
18 ensation of serine with homocysteine to form cystathionine and occupies a crucial regulatory position
19 ct in SAA metabolism: homocystine, cysteine, cystathionine and serine were significantly decreased in
22 ay, one-carbon metabolism, transsulfuration (cystathionine), and glycine decarboxylation (serine and
23 tration of a gamma-elimination reaction with cystathionine as well as the gamma-replacement reaction
24 s endogenously produced from homocysteine by cystathionine beta synthase (CBS) and cystathionine gamm
27 sensitivity to chemotherapeutic agents (eg, cystathionine beta synthase, dCMP deaminase, and CTP syn
28 yielded variant ALR(Y274F), which catalyzes cystathionine beta-elimination with a near-native Michae
30 us assay for the forward reaction, employing cystathionine beta-lyase and L-lactate dehydrogenase as
31 , methionine synthase reductase (MTRR A66G), cystathionine beta-synthase (CBS exon 8, 68-base-pair in
32 nate heme in the H2S-generating human enzyme cystathionine beta-synthase (CBS) acts as a redox-sensit
33 and hypercholesterolemia in which the mouse cystathionine beta-synthase (CBS) and apolipoprotein E (
34 es involved in the transsulfuration pathway, cystathionine beta-synthase (CBS) and cystathionine gamm
35 wo enzymes in the trans-sulfuration pathway, cystathionine beta-synthase (CBS) and cystathionine gamm
36 synthesized by the transsulfuration enzymes cystathionine beta-synthase (CBS) and cystathionine gamm
38 zed by the transsulfuration pathway enzymes, cystathionine beta-synthase (CBS) and gamma-cystathionas
39 Hcy and hyperlipidemia mouse model, in which cystathionine beta-synthase (CBS) and low-density lipopr
50 e setting of hyperhomocysteinemia because of cystathionine beta-synthase (CBS) deficiency, an inborn
51 Homocystinuria, which typically results from cystathionine beta-synthase (CBS) deficiency, is the mos
53 e of CNNM2 (CNNM2BAT), which consists of two cystathionine beta-synthase (CBS) domains (IPR000664) an
55 rous proteins containing pairs of regulatory cystathionine beta-synthase (CBS) domains, family II pyr
56 cleotide-binding insert comprising a pair of cystathionine beta-synthase (CBS) domains, termed a Bate
59 serine hydroxymethyltransferase (SHMT), and cystathionine beta-synthase (CBS) genes and their associ
60 onine synthase (MS), MS reductase (MSR), and cystathionine beta-synthase (CBS) in the NCI60 panel of
74 omocysteinemia due to genetic alterations in cystathionine beta-synthase (Cbs) or methylenetetrahydro
75 dition to elevating plasma Hcy, mutations in cystathionine beta-synthase (CBS) or methylenetetrahydro
77 nism, unique to breast cancer cells, whereby cystathionine beta-synthase (CBS) promotes elevated GSH/
81 ine clearance converge at the active site of cystathionine beta-synthase (CBS), a pyridoxal phosphate
82 Patients with homocystinuria lack the enzyme cystathionine beta-synthase (CBS), and many of these ind
83 gen sulfide (H2S) producing enzymes, namely, cystathionine beta-synthase (CBS), cystathionine gamma l
84 d metabolism caused by deficient activity of cystathionine beta-synthase (CBS), resulting in an accum
85 mitting step in this pathway is catalyzed by cystathionine beta-synthase (CBS), which is subject to c
90 ound a single nucleotide polymorphism within cystathionine beta-synthase (CYS4) that causes multi-dru
93 1298A>C, methionine synthase [MTR] 2756A>G, cystathionine beta-synthase [CBS] 844ins68, and methioni
95 zMC), serves as a highly sensitive assay for cystathionine beta-synthase activity, and is suitable fo
96 ons from the models, mutation of residues in cystathionine beta-synthase and channel domains either a
97 hide (H2S), through multiple steps involving cystathionine beta-synthase and cystathionine gamma-lyas
98 oduced endogenously by catalytic activity of cystathionine beta-synthase and cystathionine gamma-lyas
100 zed by the transsulfuration pathway enzymes, cystathionine beta-synthase and cystathionine gamma-lyas
101 the human transsulfuration pathway enzymes, cystathionine beta-synthase and gamma-cystathionase (CSE
102 of MST versus the other two H2S generators, cystathionine beta-synthase and gamma-cystathionase, has
103 es the cytoplasmic transsulfuration enzymes, cystathionine beta-synthase and gamma-cystathionase, whe
106 oprotection, its chronic increase such as in cystathionine beta-synthase deficiency may pose a proble
108 e and stability of PAE2072, a dimeric tandem cystathionine beta-synthase domain protein from the hype
111 -phosphate isomerases but lacking the tandem cystathionine beta-synthase domains found in the other a
112 eep in a cleft formed by ClC-1 intracellular cystathionine beta-synthase domains, and the nicotinamid
113 rase domain of E. coli KdsD, lacking the two cystathionine beta-synthase domains, demonstrated API ac
117 eterozygous for a targeted disruption of the cystathionine beta-synthase gene (Cbs+/-) and wild-type
122 vels of UNG mRNA were increased in brains of cystathionine beta-synthase knockout mice, a model for h
123 it was reversed by the inhibition of either cystathionine beta-synthase or cystathionine gamma-lyase
125 Here we express a mutant form of the human cystathionine beta-synthase protein, I278T, in Saccharom
127 xample of mutations in the catalytic core of cystathionine beta-synthase that result in failure of Ad
128 oderate (88 micromol/L) HHcy were induced in cystathionine beta-synthase wild-type (Cbs(+/+)) and het
129 ilarly, a particular M.grisea CBS1 (encoding cystathionine beta-synthase) TAGKO cDNA failed to comple
131 osome binding site of the cbs gene, encoding cystathionine beta-synthase, an enzyme that is a part of
132 we demonstrate that inactivation of putative cystathionine beta-synthase, cystathionine gamma-lyase,
134 OR1 induction resulted in down-regulation of Cystathionine beta-synthase, which is known to lead to i
135 h-density lipoprotein cholesterol (HDL-C) in cystathionine beta-synthase-/apolipoprotein E-deficient
138 einylation impairs collagen cross-linking in cystathionine beta-synthase-deficient mice: a novel mech
139 In hyperhomocysteinemic human cells and cystathionine beta-synthase-deficient mouse brains, we f
140 PON1 affects plasma N-Hcy-protein levels in cystathionine beta-synthase-deficient patients (n=28).
147 the abundance of the transsulfuration enzyme cystathionine beta-synthase; treatment of diabetic rats
148 ogenous hydrogen sulfide synthesizing enzyme cystathionine beta-synthetase (CBS) in sensitization of
149 approximately 150 muM), which was induced in cystathionine-beta synthase heterozygous mice fed a high
152 emic mice deficient in the Cbs gene encoding cystathionine-beta-synthase (Cbs(+/-)) to evaluate retin
155 Individuals with homozygous deficiency in cystathionine-beta-synthase (CBS) develop high levels of
156 requires ATP, which binds to the C-terminal cystathionine-beta-synthase (CBS) domain of SpoIVFB.
159 ficiency or absence of the cbs gene encoding cystathionine-beta-synthase (CBS) have marked retinal di
160 ve up-regulation of the H2S-producing enzyme cystathionine-beta-synthase (CBS) in colon cancer, resul
161 e-homocysteine methyltransferase (Bhmt), and cystathionine-beta-synthase (Cbs) were up-regulated, but
163 thionine adenosyltransferase 1alpha (Mat1a), cystathionine-beta-synthase (Cbs), methylenetetrahydrofo
164 heterozygous for disruption of the gene for cystathionine-beta-synthase (Cbs+/-) and C57BL/6 (Cbs+/+
165 ntracellular carboxy-terminus containing two cystathionine-beta-synthase (CBS1 and CBS2) domains.
166 yperhomocysteinemia induced in wild-type and cystathionine-beta-synthase +/- mice by feeding a high-m
168 ysteine by reverse transsulfurylation with a cystathionine-beta-synthase and cystathionine-gamma-lyas
171 rt or deletion of the last 11 amino acids of cystathionine-beta-synthase domain 1 gives rise to funct
173 d large cytoplasmic C-termini containing two cystathionine-beta-synthase domains (CBS1 and CBS2) that
175 s proposed in which mutagenesis is driven by cystathionine-beta-synthase overexpression and altered f
176 that ox-LDL treatment down-regulated the H2S/cystathionine-beta-synthase pathway, with increased MCP-
177 inically relevant AML cell line models, high cystathionine-beta-synthase transcripts in DS CMK cells
179 ism secondary to genes on chromosome 21 (eg, cystathionine-beta-synthase, superoxide dismutase) as po
180 ression of the gene, designated M truncatula Cystathionine-beta-Synthase-like1 (MtCBS1), using a prom
183 bosylhomocysteine, homocysteine, methionine, cystathionine, cysteine, and homoserine were quantified
184 homocysteine (SAH), adenosine, homocysteine, cystathionine, cysteine, and oxidized and reduced glutat
185 entrations of methionine, SAM, homocysteine, cystathionine, cysteine, and total glutathione and signi
186 oline, phosphocholine, glyceophosphocholine, cystathionine, cysteine, hydrogen sulfide, glutathione d
188 rom the methionine cycle provides sulfur for cystathionine formation, which may subsequently be used
190 In the reverse direction, CBS reacted with cystathionine, forming the aminoacrylate intermediate wi
192 , namely, cystathionine beta-synthase (CBS), cystathionine gamma lyase (CSE) and 3-mercaptopyruvate s
194 H(2)S by cardiac-specific overexpression of cystathionine gamma-lyase (alpha-MHC-CGL-Tg mouse) signi
195 Cardiomyocyte-specific overexpression of cystathionine gamma-lyase (an enzyme that produces H(2)S
196 of the transsulfuration pathway (TSP) enzyme cystathionine gamma-lyase (CGL), resulting in increased
200 rived vasodilator, is produced by the enzyme cystathionine gamma-lyase (CSE) and acts by hyperpolariz
202 rates, cystathionine beta-synthase (CBS) and cystathionine gamma-lyase (CSE) are enzymes that catalys
203 on and activity of the H2S-generating enzyme cystathionine gamma-lyase (CSE) by promoting its transla
204 ect enzymatically produced H2S from isolated cystathionine gamma-lyase (CSE) enzymes (p < 0.001) and
205 d that mice lacking the H2S-producing enzyme cystathionine gamma-lyase (CSE) exhibit elevated oxidati
212 e of O2 sensing in the carotid body, express cystathionine gamma-lyase (CSE), an H2S-generating enzym
213 thway, cystathionine beta-synthase (CBS) and cystathionine gamma-lyase (CSE), are believed to be chie
214 since mice lacking its biosynthetic enzyme, cystathionine gamma-lyase (CSE), display pronounced hype
215 thway, cystathionine beta-synthase (CBS) and cystathionine gamma-lyase (CSE), H2S has been implicated
216 H2S), a gaseous messenger produced mainly by cystathionine gamma-lyase (CSE), is a proangiogenic vaso
219 ne K(M) and V(max) for natural substrates of cystathionine gamma-lyase (CSE), the main enzyme respons
220 rom ischemia/reperfusion injury, but whether cystathionine gamma-lyase (CSE), which produces endogeno
229 ls to make H(2)S via increased expression of cystathionine gamma-lyase and cystathionine beta-synthas
234 genous expression of various KAT enzymes and cystathionine gamma-lyase present in target tissue coupl
236 evented by propargylglycine, an inhibitor of cystathionine gamma-lyase that catalyzes H(2)S formation
238 uation, immunohistochemistry (nitrotyrosine, cystathionine gamma-lyase, activated caspase-3, and extr
239 l content of cystathionine beta-synthase and cystathionine gamma-lyase, hydrogen sulfide-generating e
240 ion of putative cystathionine beta-synthase, cystathionine gamma-lyase, or 3-mercaptopyruvate sulfurt
244 i) seeds with lower transcript expression of CYSTATHIONINE gamma-SYNTHASE (AtCGS), Met's main regulat
245 duces O-phospho-l-homoserine (HserP) used by cystathionine gamma-synthase (CGS) for Met synthesis and
247 079, annotated metB, was predicted to encode cystathionine gamma-synthase (CGS), but demonstration of
250 sent study aimed to identify the presence of cystathionine-gamma-lyase (CSE) and 3-mercaptopyruvate s
251 overexpression of the H(2)S-producing enzyme cystathionine-gamma-lyase (CSE) attenuated the hyperglyc
252 e in vascular beds, and its synthetic enzyme cystathionine-gamma-lyase (CSE) is down-regulated in gro
254 etic ablation of the H2S-synthesizing enzyme cystathionine-gamma-lyase (CSE) normalized breathing in
256 7 and propargylglycin (PAG), an inhibitor of cystathionine-gamma-lyase (CSE), a key enzyme that produ
259 This study investigated the activities of cystathionine-gamma-lyase (CSE, the enzyme that catalyze
261 ocker, 1 mg/kg) or dl-propargylglycine (PAG, Cystathionine-gamma-lyase [CSE, H(2)S-producing enzyme]
262 ely, silencing of the H(2)S-producing enzyme cystathionine-gamma-lyase abolishes NO-stimulated cGMP a
263 responsible for endogenous H2 S production, cystathionine-gamma-lyase and 3-mercaptopyruvate sulphur
264 the carotid body requires the interaction of cystathionine-gamma-lyase with haem oxygenase-2, which g
265 These include cystathionine beta-synthase, cystathionine-gamma-lyase, paraxonase 1, 5,10-methylenet
266 e carotid body, express haem oxygenase-2 and cystathionine-gamma-lyase, the enzymes which catalyse th
268 hese reactions are catalyzed by irreversible cystathionine-gamma-synthase and cystathionine-beta-lyas
269 ds expressing a feedback-insensitive form of CYSTATHIONINE-gamma-SYNTHASE, a key enzyme of Met synthe
270 his study aimed to explore whether and how L-cystathionine had any regulatory effect on the inflammat
273 splaced by the thiol of L-cysteine to form L-cystathionine, in the first step of the bacterial transs
274 t condenses serine with homocysteine to form cystathionine; intriguingly, human CBS also contains a h
275 and cell-culture models, we have found that cystathionine is capable of blocking the induction of he
278 of the first of two enzymes in this pathway, cystathionine, is present at higher levels in brain as c
279 y the thiol of homocysteine (L-Hcys) to form cystathionine (L-Cth) in the first step of the trans-sul
280 ysis indicate that the protective effects of cystathionine occur without any obvious alteration of th
282 Currently there is no known function for cystathionine other than serving as an intermediate in t
283 c acid (P<0.01-0.04), homocysteine (P<0.01), cystathionine (P<0.01), and the decreased S-adenosylmeth
286 l as the gamma-replacement reaction yielding cystathionine showed it encodes a bifunctional CGL/CGS e
287 he ox-LDL group, 0.3 mmol/L and 1.0 mmol/L L-cystathionine significantly inhibited the expression of
288 t enzymes involved in L-cysteine metabolism: cystathionine-ss-synthase (CBS) and cystathionine-gamma-
289 Mechanistically, 0.3 mmol/L and 1.0 mmol/L L-cystathionine suppressed phosphorylation and nuclear tra
290 experimental evidence that the abolition of cystathionine synthesis may contribute to the pathology
291 he possible contribution of the abolition of cystathionine synthesis to pathogenesis in HCU has not b
294 regulates these competing reactions where by cystathionine, the product of CBS, inhibits H2S synthesi
295 ion of homocysteine into Dha formed a stable cystathionine (thioether) analogue of the complement inh
297 1, flip the operating preference of CSE from cystathionine to cysteine, transiently stimulating H2S p
298 ha-ketoglutarate, asparagine, aspartic acid, cystathionine, total cysteine, glutamic acid, glutamine,
299 homoserine via its sulfhydryl group to form cystathionine, which is cleaved to yield homocysteine.
300 CBS condenses serine and homocysteine to cystathionine with the help of three cofactors, heme, py
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