Information on EC 3.1.1.78 - polyneuridine-aldehyde esterase

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The expected taxonomic range for this enzyme is: Rauvolfia serpentina

EC NUMBER
COMMENTARY hide
3.1.1.78
-
RECOMMENDED NAME
GeneOntology No.
polyneuridine-aldehyde esterase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
polyneuridine aldehyde + H2O = 16-epivellosimine + CO2 + methanol
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
ester hydrolysis
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ajmaline and sarpagine biosynthesis
-
-
Indole alkaloid biosynthesis
-
-
Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
polyneuridine aldehyde hydrolase (decarboxylating)
Following hydrolysis of this indole alkaloid ester the carboxylic acid decarboxylates spontaneously giving the sarpagan skeleton. The enzyme also acts on akuammidine aldehyde (the 16-epimer of polyneuridine aldehyde).
CAS REGISTRY NUMBER
COMMENTARY hide
87041-55-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Rauvolfia serpentina Benth. ex Kurz
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
akuammidine aldehyde + H2O
vellosiminol + CO2 + methanol
show the reaction diagram
Rauvolfia serpentina Benth. ex Kurz
-
-
-
-
?
polyneuridine aldehyde + H2O
16-epivellosimine + CO2 + methanol
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
polyneuridine aldehyde + H2O
16-epivellosimine + CO2 + methanol
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dithiodipyridine
Rauvolfia serpentina Benth. ex Kurz
-
-
5,5'-dithio-bis-(2-nitrobenzoate)
Rauvolfia serpentina Benth. ex Kurz
-
-
diethyldicarbonate
Rauvolfia serpentina Benth. ex Kurz
-
100% inhibition at 0.8 mM
HgCl2
Rauvolfia serpentina Benth. ex Kurz
-
100% inhibition at 0.2 mM
iodoacetamide
Rauvolfia serpentina Benth. ex Kurz
-
100% inhibition at 5 mM
L-chloro-3-[4-tosyl-amido]-7-amido-2-heptanone
Rauvolfia serpentina Benth. ex Kurz
-
12% inhibition at 0.12 mM
MgCl2
Rauvolfia serpentina Benth. ex Kurz
-
50% inhibition at 0.25 mM
MnCl2
Rauvolfia serpentina Benth. ex Kurz
-
50% inhibition at 0.25 mM
phenylmethanesulfonyl fluoride
Rauvolfia serpentina Benth. ex Kurz
-
20% inhibition at 1 mM
ZnCl2
Rauvolfia serpentina Benth. ex Kurz
-
50% inhibition at 0.25 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.83 - 1.25
polyneuridine aldehyde
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
Rauvolfia serpentina Benth. ex Kurz
-
-
8
Rauvolfia serpentina Benth. ex Kurz
-
assay conditions
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8.5
Rauvolfia serpentina Benth. ex Kurz
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
Rauvolfia serpentina Benth. ex Kurz
-
assay conditions
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
Rauvolfia serpentina Benth. ex Kurz
-
2 * 30000, SDS-PAGE
60000
Rauvolfia serpentina Benth. ex Kurz
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Rauvolfia serpentina Benth. ex Kurz
-
2 * 30000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the core domain of PNAE consists of six beta sheets flanked by five alpha helices and the cap domain. The opening of the reaction channel is located in the cap, a region which in contrast to the canonical core of the alpha/beta hydrolases, is structurally highly flexible
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, 5 months, 0.2 M 2-mercaptoethanol, 100% activity
Rauvolfia serpentina Benth. ex Kurz
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Rauvolfia serpentina Benth. ex Kurz
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15
Rauvolfia serpentina Benth. ex Kurz
-
fused with a C-terminal His-tag
Rauvolfia serpentina Benth. ex Kurz
-
overexpressed in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H244A
mutant shows extremely reduced hydrolase activity. Crystal structure of His244Ala in complex with the enzyme product: the indolic part in the molecule interacts with Met113, Phe125, Tyr128, and Lys187. This arrangement enables the alkaloid to be fixed by hydrophobic, sandwichlike interactions providing optimal structural accommodation for catalysis
H86A
mutant shows extremely reduced hydrolase activity. Like Met245, His86 is far from the water molecules in the active center. It might therefore be of structural rather than of catalytic significance
M245A
mutant shows extremely reduced hydrolase activity. Met245 is far from the water molecules in the active center and as the neighbor residue of the catalytic His244, it might therefore be of structural rather than of catalytic significance
C132A
Rauvolfia serpentina Benth. ex Kurz
-
755% lower activity than wild-type
C170A
Rauvolfia serpentina Benth. ex Kurz
-
80% lower activity than wild-type
C213S/G152Q
Rauvolfia serpentina Benth. ex Kurz
-
35% lower activity than wild-type
C257A
Rauvolfia serpentina Benth. ex Kurz
-
35% lower activity than wild-type
H17A
Rauvolfia serpentina Benth. ex Kurz
-
97% lower activity than wild-type