Literature references that cite this PDB file's
key reference
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PubMed id
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Reference
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C.A.Opere,
E.M.Monjok,
K.H.Kulkarni,
Y.F.Njie,
and
S.E.Ohia
(2009).
Regulation of [(3)h] d: -aspartate release from mammalian isolated retinae by hydrogen sulfide.
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Neurochem Res, 34,
1962-1968.
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K.H.Kulkarni,
E.M.Monjok,
R.Zeyssig,
G.Kouamou,
O.N.Bongmba,
C.A.Opere,
Y.F.Njie,
and
S.E.Ohia
(2009).
Effect of hydrogen sulfide on sympathetic neurotransmission and catecholamine levels in isolated porcine iris-ciliary body.
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Neurochem Res, 34,
400-406.
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L.R.Singh,
and
W.D.Kruger
(2009).
Functional Rescue of Mutant Human Cystathionine {beta}-Synthase by Manipulation of Hsp26 and Hsp70 Levels in Saccharomyces cerevisiae.
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J Biol Chem, 284,
4238-4245.
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M.Sieńko,
R.Natorff,
S.Owczarek,
I.Olewiecki,
and
A.Paszewski
(2009).
Aspergillus nidulans genes encoding reverse transsulfuration enzymes belong to homocysteine regulon.
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Curr Genet, 55,
561-570.
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R.A.Williams,
G.D.Westrop,
and
G.H.Coombs
(2009).
Two pathways for cysteine biosynthesis in Leishmania major.
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Biochem J, 420,
451-462.
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T.Shintani,
T.Iwabuchi,
T.Soga,
Y.Kato,
T.Yamamoto,
N.Takano,
T.Hishiki,
Y.Ueno,
S.Ikeda,
T.Sakuragawa,
K.Ishikawa,
N.Goda,
Y.Kitagawa,
M.Kajimura,
K.Matsumoto,
and
M.Suematsu
(2009).
Cystathionine beta-synthase as a carbon monoxide-sensitive regulator of bile excretion.
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Hepatology, 49,
141-150.
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M.A.Grillo,
and
S.Colombatto
(2008).
S-adenosylmethionine and its products.
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Amino Acids, 34,
187-193.
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T.Majtan,
L.R.Singh,
L.Wang,
W.D.Kruger,
and
J.P.Kraus
(2008).
Active Cystathionine {beta}-Synthase Can Be Expressed in Heme-free Systems in the Presence of Metal-substituted Porphyrins or a Chemical Chaperone.
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J Biol Chem, 283,
34588-34595.
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V.Brancaleone,
F.Roviezzo,
V.Vellecco,
L.De Gruttola,
M.Bucci,
and
G.Cirino
(2008).
Biosynthesis of H2S is impaired in non-obese diabetic (NOD) mice.
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Br J Pharmacol, 155,
673-680.
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H.M.Girvan,
H.E.Seward,
H.S.Toogood,
M.R.Cheesman,
D.Leys,
and
A.W.Munro
(2007).
Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3.
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J Biol Chem, 282,
564-572.
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PDB codes:
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J.O.Rosado,
M.Salvador,
and
D.Bonatto
(2007).
Importance of the trans-sulfuration pathway in cancer prevention and promotion.
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Mol Cell Biochem, 301,
1.
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L.R.Singh,
X.Chen,
V.Kozich,
and
W.D.Kruger
(2007).
Chemical chaperone rescue of mutant human cystathionine beta-synthase.
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Mol Genet Metab, 91,
335-342.
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S.Singh,
P.Madzelan,
and
R.Banerjee
(2007).
Properties of an unusual heme cofactor in PLP-dependent cystathionine beta-synthase.
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Nat Prod Rep, 24,
631-639.
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D.Johansen,
K.Ytrehus,
and
G.F.Baxter
(2006).
Exogenous hydrogen sulfide (H2S) protects against regional myocardial ischemia-reperfusion injury--Evidence for a role of K ATP channels.
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Basic Res Cardiol, 101,
53-60.
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D.K.Simanshu,
H.S.Savithri,
and
M.R.Murthy
(2006).
Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation.
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J Biol Chem, 281,
39630-39641.
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PDB codes:
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C.G.Zou,
and
R.Banerjee
(2005).
Homocysteine and redox signaling.
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Antioxid Redox Signal, 7,
547-559.
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J.H.Schafer,
T.A.Glass,
J.Bressler,
A.C.Todd,
and
B.S.Schwartz
(2005).
Blood lead is a predictor of homocysteine levels in a population-based study of older adults.
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Environ Health Perspect, 113,
31-35.
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K.H.Jhee,
and
W.D.Kruger
(2005).
The role of cystathionine beta-synthase in homocysteine metabolism.
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Antioxid Redox Signal, 7,
813-822.
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E.W.Miles,
and
J.P.Kraus
(2004).
Cystathionine beta-synthase: structure, function, regulation, and location of homocystinuria-causing mutations.
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J Biol Chem, 279,
29871-29874.
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M.H.Stipanuk
(2004).
Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine.
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Annu Rev Nutr, 24,
539-577.
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S.Pavlovic,
M.Kuzmanovic,
J.Urosevic,
J.Poznanic,
T.Zoranovic,
V.Djordjevic,
N.Rasovic,
G.Bunjevacki,
M.Cvorkov-Drazic,
and
M.Colovic
(2004).
Severe central nervous system thrombotic events in hemoglobin Sabine patient.
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Eur J Haematol, 72,
67-70.
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C.G.Zou,
and
R.Banerjee
(2003).
Tumor necrosis factor-alpha-induced targeted proteolysis of cystathionine beta-synthase modulates redox homeostasis.
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J Biol Chem, 278,
16802-16808.
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K.Mino,
and
K.Ishikawa
(2003).
Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1.
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J Bacteriol, 185,
2277-2284.
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K.Mino,
Y.Oda,
M.Ataka,
and
K.Ishikawa
(2003).
Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1.
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Acta Crystallogr D Biol Crystallogr, 59,
338-340.
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R.Omi,
M.Goto,
I.Miyahara,
H.Mizuguchi,
H.Hayashi,
H.Kagamiyama,
and
K.Hirotsu
(2003).
Crystal structures of threonine synthase from Thermus thermophilus HB8: conformational change, substrate recognition, and mechanism.
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J Biol Chem, 278,
46035-46045.
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PDB codes:
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T.Ose,
A.Fujino,
M.Yao,
N.Watanabe,
M.Honma,
and
I.Tanaka
(2003).
Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction.
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J Biol Chem, 278,
41069-41076.
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PDB codes:
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T.Yamada,
J.Komoto,
Y.Takata,
H.Ogawa,
H.C.Pitot,
and
F.Takusagawa
(2003).
Crystal structure of serine dehydratase from rat liver.
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Biochemistry, 42,
12854-12865.
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PDB codes:
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B.Deplancke,
and
H.R.Gaskins
(2002).
Redox control of the transsulfuration and glutathione biosynthesis pathways.
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Curr Opin Clin Nutr Metab Care, 5,
85-92.
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J.Oliveriusová,
V.Kery,
K.N.Maclean,
and
J.P.Kraus
(2002).
Deletion mutagenesis of human cystathionine beta-synthase. Impact on activity, oligomeric status, and S-adenosylmethionine regulation.
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J Biol Chem, 277,
48386-48394.
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M.Gaustadnes,
B.Wilcken,
J.Oliveriusova,
J.McGill,
J.Fletcher,
J.P.Kraus,
and
D.E.Wilcken
(2002).
The molecular basis of cystathionine beta-synthase deficiency in Australian patients: genotype-phenotype correlations and response to treatment.
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Hum Mutat, 20,
117-126.
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S.C.Lo,
L.Hamer,
and
J.E.Hamer
(2002).
Molecular characterization of a cystathionine beta-synthase gene, CBS1, in Magnaporthe grisea.
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Eukaryot Cell, 1,
311-314.
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S.Taoka,
and
R.Banerjee
(2002).
Stopped-flow kinetic analysis of the reaction catalyzed by the full-length yeast cystathionine beta-synthase.
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J Biol Chem, 277,
22421-22425.
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V.A.Bamford,
S.Bruno,
T.Rasmussen,
C.Appia-Ayme,
M.R.Cheesman,
B.C.Berks,
and
A.M.Hemmings
(2002).
Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme.
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EMBO J, 21,
5599-5610.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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348 a.a.
]positions. The substrate analog of OASS methionine indicates the probable binding mode of the first substrate serine and also the region where the second substrate homocysteine is expected to bind. (B) The heme binding site of CBS with heme in green and the surrounding residues in gray. The two residues His65 and Cys52 are the ligands to the heme iron (dark red). The difference density for the cofactor is shown in red contoured at 3.5
. (C) The oxidoreductase motif in ball-and-stick representation and (D) in a superposition with the structure of glutaredoxin. The structure of CBS is in gray, the one of glutaredoxin in green. The overall topology is very similar, but the active site motif in CBS is switched to the other helix compared with glutaredoxin.
