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PDBsum entry 4zoh
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Oxidoreductase
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PDB id
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4zoh
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Contents |
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701 a.a.
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274 a.a.
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161 a.a.
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References listed in PDB file
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Key reference
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Title
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Archaeal mo-Containing glyceraldehyde oxidoreductase isozymes exhibit diverse substrate specificities through unique subunit assemblies.
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Authors
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T.Wakagi,
H.Nishimasu,
M.Miyake,
S.Fushinobu.
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Ref.
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Plos One, 2016,
11,
e0147333.
[DOI no: ]
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PubMed id
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Abstract
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Archaea use glycolytic pathways distinct from those found in bacteria and
eukaryotes, where unique enzymes catalyze each reaction step. In this study, we
isolated three isozymes of glyceraldehyde oxidoreductase (GAOR1, GAOR2 and
GAOR3) from the thermoacidophilic archaeon Sulfolobus tokodaii. GAOR1-3 belong
to the xanthine oxidoreductase superfamily, and are composed of a
molybdo-pyranopterin subunit (L), a flavin subunit (M), and an iron-sulfur
subunit (S), forming an LMS hetero-trimer unit. We found that GAOR1 is a
tetramer of the STK17810/STK17830/STK17820 hetero-trimer, GAOR2 is a dimer of
the STK23390/STK05620/STK05610 hetero-trimer, and GAOR3 is the
STK24840/STK05620/STK05610 hetero-trimer. GAOR1-3 exhibited diverse substrate
specificities for their electron donors and acceptors, due to their different
L-subunits, and probably participate in the non-phosphorylative Entner-Doudoroff
glycolytic pathway. We determined the crystal structure of GAOR2, as the first
three-dimensional structure of an archaeal molybdenum-containing hydroxylase, to
obtain structural insights into their substrate specificities and subunit
assemblies. The gene arrangement and the crystal structure suggested that the
M/S-complex serves as a structural scaffold for the binding of the L-subunit, to
construct the three enzymes with different specificities. Collectively, our
findings illustrate a novel principle of a prokaryotic multicomponent isozyme
system.
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Secondary reference #1
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Title
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A novel bifunctional molybdo-Enzyme catalyzing both decarboxylation of indolepyruvate and oxidation of indoleacetaldehyde from a thermoacidophilic archaeon, Sulfolobus sp. Strain 7.
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Authors
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T.Wakagi,
E.Fukuda,
Y.Ogawa,
H.Kino,
H.Matsuzawa.
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Ref.
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Febs Lett, 2002,
510,
196-200.
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PubMed id
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