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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biological process
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carbohydrate metabolic process
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1 term
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Biochemical function
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catalytic activity
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3 terms
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DOI no:
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Plant Cell
19:2886-2897
(2007)
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PubMed id:
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Molecular architecture of strictosidine glucosidase: the gateway to the biosynthesis of the monoterpenoid indole alkaloid family.
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L.Barleben,
S.Panjikar,
M.Ruppert,
J.Koepke,
J.Stöckigt.
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ABSTRACT
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Strictosidine beta-D-glucosidase (SG) follows strictosidine synthase (STR1) in
the production of the reactive intermediate required for the formation of the
large family of monoterpenoid indole alkaloids in plants. This family is
composed of approximately 2000 structurally diverse compounds. SG plays an
important role in the plant cell by activating the glucoside strictosidine and
allowing it to enter the multiple indole alkaloid pathways. Here, we report
detailed three-dimensional information describing both native SG and the complex
of its inactive mutant Glu207Gln with the substrate strictosidine, thus
providing a structural characterization of substrate binding and identifying the
amino acids that occupy the active site surface of the enzyme. Structural
analysis and site-directed mutagenesis experiments demonstrate the essential
role of Glu-207, Glu-416, His-161, and Trp-388 in catalysis. Comparison of the
catalytic pocket of SG with that of other plant glucosidases demonstrates the
structural importance of Trp-388. Compared with all other glucosidases of plant,
bacterial, and archaeal origin, SG's residue Trp-388 is present in a unique
structural conformation that is specific to the SG enzyme. In addition to STR1
and vinorine synthase, SG represents the third structural example of enzymes
participating in the biosynthetic pathway of the Rauvolfia alkaloid ajmaline.
The data presented here will contribute to deciphering the structure and
reaction mechanism of other higher plant glucosidases.
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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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J.R.Ketudat Cairns,
and
A.Esen
(2010).
β-Glucosidases.
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Cell Mol Life Sci, 67,
3389-3405.
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L.Yang,
and
J.Stöckigt
(2010).
Trends for diverse production strategies of plant medicinal alkaloids.
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Nat Prod Rep, 27,
1469-1479.
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P.Bernhardt,
N.Yerkes,
and
S.E.O'Connor
(2009).
Bypassing stereoselectivity in the early steps of alkaloid biosynthesis.
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Org Biomol Chem, 7,
4166-4168.
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J.Ziegler,
and
P.J.Facchini
(2008).
Alkaloid biosynthesis: metabolism and trafficking.
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Annu Rev Plant Biol, 59,
735-769.
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N.Yerkes,
J.X.Wu,
E.McCoy,
M.C.Galan,
S.Chen,
and
S.E.O'Connor
(2008).
Substrate specificity and diastereoselectivity of strictosidine glucosidase, a key enzyme in monoterpene indole alkaloid biosynthesis.
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Bioorg Med Chem Lett, 18,
3095-3098.
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P.J.Facchini,
and
V.De Luca
(2008).
Opium poppy and Madagascar periwinkle: model non-model systems to investigate alkaloid biosynthesis in plants.
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Plant J, 54,
763-784.
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J.Stöckigt,
and
S.Panjikar
(2007).
Structural biology in plant natural product biosynthesis--architecture of enzymes from monoterpenoid indole and tropane alkaloid biosynthesis.
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Nat Prod Rep, 24,
1382-1400.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
