Information on EC 3.2.1.105 - 3alpha(S)-strictosidine beta-glucosidase

655431, 713606, 751210

Substrates: -
Products: -

strictosidine + H2O

D-glucose + strictosidine aglycone

714624

Substrates: specific substrate
Products: -

strictosidine + H2O

D-glucose + strictosidine aglycone

Substrates: -
Products: -

strictosidine + H2O

D-glucose + strictosidine aglycone

Substrates: -
Products: -

strictosidine + H2O

D-glucose + strictosidine aglycone

Substrates: -
Products: the major intermediate after rearrangement of the strictosidine aglycone is thought to be 21-hydroxyajmalicine

strictosidine + H2O

D-glucose + strictosidine aglycone

Uncaria tomentosa

I6ZQ42

729484

Substrates: -
Products: -

additional information

Substrates: involved In the indole alkaloid biosynthesis by hydrolyzing strictosidine to cathenamine
Products: -

additional information

Substrates: no substrates: strictosidine pentaacetate, vincoside, strictosidine lactam, vincoside lactam, raucafficrine, 1,2-dihydrocafficrine, 1-methyl-1,2-dihydrocarcafficrine, secologanin, loganin, 4-nitrophenylglucoside, arbutin, vanillin-glucoside, isatinoxim-glucoside, prunasin, rhapontin, rutin, sinigrin and zeatin-glucoside
Products: -

additional information

additional information

713606

Substrates: the enzyme does not accept raucaffricine as substrate
Products: -

additional information

Substrates: no activity with secologanin, strictosamide or p-nitrophenyl-beta-D-glucopyranoside
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

strictosidine

3 entries

strictosidine + H2O

D-glucose + strictosidine aglycone

additional information

Substrates: involved In the indole alkaloid biosynthesis by hydrolyzing strictosidine to cathenamine
Products: -

strictosidine

Substrates: -
Products: -

strictosidine

Substrates: the enzyme may play an important role in steering the monoterpenoid indole alkaloid biosynthesis in a specific direction
Products: -

strictosidine

Substrates: enzyme in terpenoid indole alkaloid biosynthesis
Products: -

strictosidine + H2O

D-glucose + strictosidine aglycone

731951

Substrates: -
Products: -

strictosidine + H2O

D-glucose + strictosidine aglycone

710520

Substrates: -
Products: i.e. hemiacetal

strictosidine + H2O

D-glucose + strictosidine aglycone

Substrates: -
Products: -

strictosidine + H2O

D-glucose + strictosidine aglycone

Uncaria tomentosa

I6ZQ42

729484

Substrates: -
Products: -

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

Cu2+

D(+)-gluconic acid delta-lactone

D-gluconolactone

N-(bromobenzyl)-beta-D-gluco-1,5-deoxa-pyranosylamine

the inhibitor anchors exclusively in the catalytic active site by competition with appropriate enzyme substrates

N-(cyclohexylmethyl)-beta-D-gluco-1,5-deoxa-pyranosylamine

the inhibitor anchors exclusively in the catalytic active site by competition with appropriate enzyme substrates

serpentine

strictosidine

enzyme I shows substrate inhibition at 1 mM, enzyme II not

tryptamine

2.5 mM, 15% inhibition of enzyme I and II

additional information

Cu2+

1 mM

Cu2+

8.8% inhibition at 1 mM

D(+)-gluconic acid delta-lactone

enzyme I is much less sensitive than enzyme II

D(+)-gluconic acid delta-lactone

some inhibition at a concentration of 10 mM and higher

D-gluconolactone

strong inhibitor

D-gluconolactone

strong inhibitor

serpentine

1 mM

serpentine

25.2% inhibition at 1 mM

additional information

enzyme activity is not inhibited by raucaffricine

713606

additional information

no inhibition by N-(cyclohexyl)-beta-D-gluco-1,5-deoxa-pyranosylamine

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.22

5-methylstrictosidine

pH 6.0, 37°C

0.15

6-fluorostrictosidine

pH 6.0, 37°C

0.37

6-methoxystrictosidine

pH 6.0, 37°C

0.071

6-methylstrictosidine

pH 6.0, 37°C

0.12

7-fluorostrictosidine

pH 6.0, 37°C

0.43

7-methoxystrictosidine

pH 6.0, 37°C

0.092

7-methylstrictosidine

pH 6.0, 37°C

0.14

8-methylstrictosidine

pH 6.0, 37°C

0.564 - 1.13

dolichantoside

0.335 - 7.015

palicoside

0.01 - 10

strictosidine

12 entries

0.564

dolichantoside

0.564

dolichantoside

pH 6.3, 30°C

1.13

dolichantoside

1.13

dolichantoside

pH 6.3, 30°C

0.335

palicoside

0.335

palicoside

pH 6.3, 30°C

7.015

palicoside

7.015

palicoside

pH 6.3, 30°C

0.01 - 0.018

strictosidine

0.018

strictosidine

0.1

strictosidine

enzyme II

0.12

strictosidine

0.12

strictosidine

pH 5, 30°C

0.12

strictosidine

pH 6.3, 30°C

0.12

strictosidine

pH and temperature not specified in the publication

713606

0.2

strictosidine

enzyme I

0.22

strictosidine

pH 6.0, 37°C

0.25 - 0.33

strictosidine

enzyme form SGIII

strictosidine

show all columns Go to Ki Value Search

above, enzyme form SGII

strictosidine

pH 6.3, 30°C

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.127

N-(bromobenzyl)-beta-D-gluco-1,5-deoxa-pyranosylamine

30°C, pH 5.0

show all columns Go to Specific Activity Search

6.7

N-(cyclohexylmethyl)-beta-D-gluco-1,5-deoxa-pyranosylamine

30°C, pH 5.0

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

additional information

additional information

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4.5 - 5

enzyme form SGI, a second pH-optimum at pH 7.0

5.2

6 - 6.4

enzyme I and II

6 - 8.5

enzyme form SGI, a second pH-optimum at pH 4.5-5.0

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4.2 - 8

50% of maximal activity at oH 4.2, above pH 5.2 the activity slowly decreases up to pH 8

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

show all columns Go to Pi Value Search

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pI VALUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

calculated from amino acid sequence

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Amsonia orientalis

weak activity

brenda

Amsonia salicifolia

brenda

Catharanthus ovalis

brenda

Catharanthus pusillus

brenda

Catharanthus trichophyllus

7 entries

brenda

weak activity

brenda

brenda

UniProt

brenda

Vinca major

weak activity

brenda

135711, 135712, 135713

brenda

UniProt

brenda

135715, 657081, 670558, 678705

brenda

714624

UniProt

brenda

brenda

UniProt

brenda

cv. Dhawal

brenda

SwissProt

brenda

667805, 705863

brenda

713606, 714624, 751210

SwissProt

brenda

brenda

cell line 59 and cell line 6B

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

brenda

brenda

brenda

abaxial and adaxial

brenda

brenda

brenda

brenda

stem

brenda

brenda

differentiation is essential for expression of acetyl-CoA: 4-O-deacetylvindoline 4-O-acetyltransferase but not strictosidine beta-D-glucosidase, overview

710520

brenda

show all columns Go to Localization Search

brenda

epidermis of aerial organs

brenda

epidermis of aerial organs

brenda

brenda

bark

brenda

brenda

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

endoplasmic reticulum

most likely associated with endoplasmic reticulum

brenda

brenda

brenda

inside the vacuole, outside of the tonoplast

5773

brenda

vacuole

inside the vacuole, outside of the tonoplast

5773

brenda

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show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

metabolism

metabolism

the enzyme catalyzes an intermediate step of terpenoid indole alkaloid biosynthesis and is involved in production of their precursor vindoline, pathway overview

710520

metabolism

the enzyme is involved in terpenoid indole alkaloids biosynthesis pathway

731951

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

Q8GU20 pBLAST

SG1_RAUSE

532

60881

Swiss-Prot

other Location (Reliability: 5)

Q9M7N7 pBLAST

Q9M7N7_CATRO

555

63043

TrEMBL

Pseudallescheria apiosperma

other Location (Reliability: 4)

A0A084GES0 pBLAST

A0A084GES0_PSEDA

2113

240826

TrEMBL

other Location (Reliability: 2)

A0A1W2TEG5 pBLAST

A0A1W2TEG5_ROSNE

Rosellinia necatrix

476

53930

TrEMBL

Pseudallescheria apiosperma

other Location (Reliability: 3)

A0A084GBX6 pBLAST

A0A084GBX6_PSEDA

476

53729

TrEMBL

Handroanthus impetiginosus

other Location (Reliability: 4)

A0A2G9H5F0 pBLAST

A0A2G9H5F0_9LAMI

9082

TrEMBL

other Location (Reliability: 2)

G8E0P8 pBLAST

G8E0P8_CAMAC

Camptotheca acuminata

532

61500

TrEMBL

other Location (Reliability: 4)

I6ZQ42 pBLAST

I6ZQ42_9GENT

Uncaria tomentosa

553

63430

TrEMBL

other Location (Reliability: 3)

M9NGS2 pBLAST

M9NGS2_RAUVE

Rauvolfia verticillata

536

61038

TrEMBL

Pseudallescheria apiosperma

Chloroplast (Reliability: 5)

A0A084GGF1 pBLAST

A0A084GGF1_PSEDA

417

48232

TrEMBL

other Location (Reliability: 2)

Go to PDB and Structure Links Search

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PDB

SCOP

CATH

UNIPROT

ORGANISM

show all columns Go to Molecular Weight Search

2jf6, download, 3D-view

2jf7, download, 3D-view

3zj7, download, 3D-view

3zj8, download, 3D-view

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

187000

enzyme form SGII, non-denaturing PAGE

190000

enzyme form SGII, non-denaturing PAGE

200000

22000

enzyme form SGII, non-denaturing PAGE

230000

enzyme I, gel filtration

250000

enzyme form I, non-denaturing PAGE

31000

enzyme form SGIII, non-denaturing PAGE

450000

500000

enzyme form II, non-denaturing PAGE

63000

630000

enzyme form III, non-denaturing PAGE

650000

native PAGE

657081

670000