Strictosidine Synthase

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<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />
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<StructureSection load='2fpb' size='350' side='right' caption='Strictosidine synthase dimer complex with tryptamine (PDB entry [[2fpb]])' scene='10/100149/Cv/3'>
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strictosidine synthase (EC 4.3.3.2) is an enzyme that catalyzes the piectet spengler chemical reaction
 
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<center> <b> tryptamine + secologanin <--> 3-alpha(S)-strictosidine + H2O </b> </center>
 
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Thus, the two substrates of this enzyme are 3-alpha(S)-strictosidine and H2O, whereas its two products are tryptamine and secologanin.
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== Function ==
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The enzyme '''strictosidine synthase''' (<scene name='Strictisidine_Synthase/Str1_sp/1'>STR1</scene>) (EC 4.3.3.2) from an Indian medicinal plant ''Rauvolfia serpentina'' is of primary importance for the biosynthetic pathway of the indole alkaloid ajmaline. STR1 initiates all biosynthetic pathways leading to the entire monoterpenoid indole alkaloid family representing an enormous structural variety of ~2000 compounds in higher plants. The enzyme is involved in the biosynthesis of all these alkaloids by catalyzing the condensation of the two initial building blocks, tryptamine and the monoterpenoid secologanin, leading to the glucoalkaloid strictosidine. The reaction type catalyzed by STR1 is so far an exceptional example in the biosynthesis of natural products. It was hitherto known only from synthetic chemistry (Pictet-Spengler–type reaction), where it is applied in alkaloid synthesis, especially of tetrahydroisoquinolines by condensation of an amine and an aldehyde under acidic conditions<ref>PMID:18280746</ref>.
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This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 3-alpha(S)-strictosidine tryptamine-lyase (secologanin-forming). Other names in common use include strictosidine synthetase, STR, and 3-alpha(S)-strictosidine tryptamine-lyase. This enzyme participates in terpenoid biosynthesis and indole and ipecac alkaloid biosynthesis.
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The overall structure of the enzyme contains a six-bladed four-stranded ß-propeller fold. All six blades are radially arranged around a pseudo six-fold symmetry axis. Each blade contains a twisted four-stranded antiparallel ß-sheet.
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== Structural highlights ==
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The <scene name='10/100149/Cv/8'>substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis</scene><ref>PMID:16531499</ref>. {{Template:ColorKey_Helix}},
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{{Template:ColorKey_Strand}},
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{{Template:ColorKey_Loop}},
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{{Template:ColorKey_Turn}}. <scene name='10/100149/Cv/9'>Active site</scene>. Water molecule are shown as red sphere.
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</StructureSection>
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==3D structures of strictosidine synthase==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[2fp8]] – sSTR1 – serpentwood<br />
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[[3v1s]] – dSTR - devilpepper<br />
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[[2fp9]] – sSTR1 + tartaric acid
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[[2fpb]] – sSTR1 (mutant) + tryptamine
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[[2fpc]] – sSTR1 + secologanin
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[[2v91]] – sSTR1 residues 32-333 + strictosidine
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[[2vaq]] – sSTR1 + inhibitor<br />
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[[6n5v]], [[7t5i]], [[7t5j]] – sSTR + indole derivative <br />
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[[4imb]], [[4iyg]] – dSTR + indole derivative <br />
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[[6s5q]], [[6s5u]], [[6s5j]], [[6s5m]] – STR + carboline derivative – ''Ophiorrhiza pumila''<br />
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[[6zea]] – STR + carboline derivative – periwinkle<br />
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== References ==
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<references/>
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[[Category: Topic Page]]

Current revision

Strictosidine synthase dimer complex with tryptamine (PDB entry 2fpb)

Drag the structure with the mouse to rotate

3D structures of strictosidine synthase

Updated on 06-December-2023

2fp8 – sSTR1 – serpentwood
3v1s – dSTR - devilpepper
2fp9 – sSTR1 + tartaric acid

2fpb – sSTR1 (mutant) + tryptamine

2fpc – sSTR1 + secologanin

2v91 – sSTR1 residues 32-333 + strictosidine

2vaq – sSTR1 + inhibitor
6n5v, 7t5i, 7t5j – sSTR + indole derivative
4imb, 4iyg – dSTR + indole derivative
6s5q, 6s5u, 6s5j, 6s5m – STR + carboline derivative – Ophiorrhiza pumila
6zea – STR + carboline derivative – periwinkle

References

  1. ↑ Stockigt J, Barleben L, Panjikar S, Loris EA. 3D-Structure and function of strictosidine synthase--the key enzyme of monoterpenoid indole alkaloid biosynthesis. Plant Physiol Biochem. 2008 Mar;46(3):340-55. doi: 10.1016/j.plaphy.2007.12.011. , Epub 2008 Jan 3. PMID:18280746 doi:http://dx.doi.org/10.1016/j.plaphy.2007.12.011
  2. ↑ Ma X, Panjikar S, Koepke J, Loris E, Stockigt J. The structure of Rauvolfia serpentina strictosidine synthase is a novel six-bladed beta-propeller fold in plant proteins. Plant Cell. 2006 Apr;18(4):907-20. Epub 2006 Mar 10. PMID:16531499 doi:10.1105/tpc.105.038018

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Santosh Panjikar, Alexander Berchansky

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