Proteopedia - User contributions [en]

Strictosidine Synthase

2008-03-06T22:03:46Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />

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.

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. The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis

Strictosidine Synthase

2008-03-06T22:01:08Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />
<scene name='Strictisidine_Synthase/Str1_sp/1'>TextToBeDisplayed</scene>
The enzyme strictosidine synthase (STR1) (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.

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. The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis

Strictosidine Synthase

2008-03-06T21:49:25Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />
The enzyme strictosidine synthase (STR1) (EC 4.3.3.2)from the 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.

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. The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis

Strictosidine Synthase

2008-03-06T21:49:00Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" /> [[Image:http://www.rcsb.org/pdb/images/2FP8_bio_r_80.jpg]]
The enzyme strictosidine synthase (STR1) (EC 4.3.3.2)from the 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.

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. The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis

Strictosidine Synthase

2008-03-06T21:48:20Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />[[Image:http://www.rcsb.org/pdb/images/2FP8_bio_r_80.jpg]]
The enzyme strictosidine synthase (STR1) (EC 4.3.3.2)from the 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.

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. The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis

Strictosidine Synthase

2008-03-06T21:47:13Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />
<img http://www.rcsb.org/pdb/images/2FP8_bio_r_80.jpg?getBest=true >
The enzyme strictosidine synthase (STR1) (EC 4.3.3.2)from the 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.

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. The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis

Strictosidine Synthase

2008-03-06T21:45:50Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />
http://www.rcsb.org/pdb/images/2FP8_bio_r_80.jpg?getBest=true
The enzyme strictosidine synthase (STR1) (EC 4.3.3.2)from the 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.

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. The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis

Strictosidine Synthase

2008-03-06T21:43:28Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />

The enzyme strictosidine synthase (STR1) (EC 4.3.3.2)from the 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.

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. The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis

Strictosidine Synthase

2008-03-06T21:42:24Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />

The enzyme strictosidine synthase (STR1) (EC 4.3.3.2)from the 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.

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. The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis
<applet load="2FPB" size="300" color="white" frame="true" align="right" spinBox="true" />

Strictosidine Synthase

2008-03-06T21:40:16Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />

The enzyme strictosidine synthase (STR1) (EC 4.3.3.2)from the 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.

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. The substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis

Strictosidine Synthase

2008-03-06T21:31:40Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />

strictosidine synthase (EC 4.3.3.2) is an enzyme that catalyzes the piectet spengler chemical reaction
<center> <b> tryptamine + secologanin <--> 3-alpha(S)-strictosidine + H2O </b> </center>

Thus, the two substrates of this enzyme are 3-alpha(S)-strictosidine and H2O, whereas its two products are tryptamine and secologanin.

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.

Strictosidine Synthase

2008-03-06T21:28:51Z

Santosh Panjikar:

<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />

strictosidine synthase (EC 4.3.3.2) is an enzyme that catalyzes the chemical reaction

3-alpha(S)-strictosidine + H2O \rightleftharpoons tryptamine + secologanin

Thus, the two substrates of this enzyme are 3-alpha(S)-strictosidine and H2O, whereas its two products are tryptamine and secologanin.

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.

Strictosidine Synthase

2008-03-06T21:24:45Z

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Proteopedia:Topic Pages

2008-03-06T21:23:08Z

Santosh Panjikar: /* Non-PDB Code Pages */

===Non-PDB Code Pages===

The list below is intended to include all pages that are not named with a PDB code, and that also have substantial content. Because this list is manually maintained, it may be out of date. For comparison, here is an automatically generated list of [[Special:Allpages/a | all pages whose titles do not begin with a numeral]], and here is a list of [[Special:Allpages | all pages]].

*[[AChE inhibitors and substrates]]
*[[Acetylcholine]]
*[[Acetylcholinesterase]]
*[[Acid-beta-glucosidase]]
*[[Antibodies]]
*[[Antizyme Inhibitor]]
*[[Bacterial Intein-Like Domains (BILs)]]
*[[DHFR]]
*[[Dihydrofolate reductase]]
*[[Eran Hodis's Favorites]]
*[[Eric Martz's Favorites]]
*[[Glycine]]
*[[Heme]]
*[[Hemoglobin]]
*[[Highest impact structures]]
*[[Hint auto-proteolytic protein-processing domains]]
*[[Matrix metalloproteinases]]
*[[P53]]
*[[Personal favorites]]
*[[SGAP]]
*[[Scene authoring tools]]
*[[Serine Protease]]
*[[Serine hydrolase]]
*[[Strictisidine Synthase]]

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===PDB Code Pages===
Here is a manually maintained list of pages titled with PDB codes that have especially well-developed content.

*[[1xjo]] Aminopeptidase
*[[1v04]] Paraoxonase-1 via directed evolution
*[[1eve]] Acetylcholinesterase complexed with the anti-Alzheimer's disease drug Aricept.