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Ligand Dhurrin

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.21

dhurrin + H2O = 4-hydroxy-(S)-mandelonitrile + beta-D-glucose

665542

-

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.85

UDP-D-glucose + (S)-4-hydroxymandelonitrile = UDP + (S)-4-hydroxymandelonitrile beta-D-glucoside

-

-

2.4.1.85

UDP-glucose + 4-hydroxymandelonitrile = UDP + (S)-4-hydroxymandelonitrile beta-D-glucoside

-

-

2.4.1.85

UDPglucose + (S)-4-hydroxymandelonitrile = UDP + (S)-4-hydroxymandelonitrile beta-D-glucoside

489458, 489461

-

2.4.1.85

3 entries

Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Substrate (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.117

dhurrin + H2O = D-glucose + 4-hydroxymandelonitrile

326271

-

3.2.1.182

dhurrin + H2O = ?

732629

-

3.2.1.21

dhurrin + H2O = (2S)-hydroxy(4-hydroxyphenyl)ethanenitrile + beta-D-glucose

719801, 722632

-

3.2.1.21

dhurrin + H2O = (S)-4-hydroxymandelonitrile + D-glucose

751824

-

3.2.1.21

dhurrin + H2O = 4-hydroxy-(S)-mandelonitrile + beta-D-glucose

665542

-

3.2.1.21

dhurrin + H2O = 4-hydroxybenzaldehyde + hydrogen cyanide + D-glucose

723352

-

3.2.1.21

dhurrin + H2O = HCN + beta-D-glucose + 4-hydroxybenzaldehyde

326271

-

3.2.1.21

5 entries

Product in Enzyme-catalyzed Reactions (3 results)

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Show Product (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.85

UDP-D-glucose + (S)-4-hydroxymandelonitrile = UDP + (S)-4-hydroxymandelonitrile beta-D-glucoside

-

-

2.4.1.85

UDP-glucose + 4-hydroxymandelonitrile = UDP + (S)-4-hydroxymandelonitrile beta-D-glucoside

-

-

2.4.1.85

UDPglucose + (S)-4-hydroxymandelonitrile = UDP + (S)-4-hydroxymandelonitrile beta-D-glucoside

4892, 489460, 489461, 489458

-

2.4.1.85

3 entries

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.85

potent inhibitor, 1 mg/ml bovine serum albumin protects

489461

-

3.2.1.182

-

720757, 720952

-

3.2.1.21

competitive inhibitor

722632

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (23 results)

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Show Turnover Number (23 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.2.1.182

52

-

recombinant enzyme, pH and temperature not specified in the publication

732629

3.2.1.21

0.16

-

pH 5.8, 37°C, mutant F205L

722632

3.2.1.21

0.21

-

pH 5.8, 37°C, mutant M263F

722632

3.2.1.21

0.55

-

pH 5.8, 37°C, mutant F466S/A467S

722632

3.2.1.21

0.59

-

pH 5.8, 37°C, mutant F466S

722632

3.2.1.21

0.7

-

pH 5.8, 37°C, mutant F198V/F205L/P377A

722632

3.2.1.21

1.13

-

pH 5.8, 37°C, mutant Y473F

722632

3.2.1.21

1.32

-

pH 5.8, 37°C, chimeric mutant (Chim21) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1

722632

3.2.1.21

2.23

-

pH 5.8, 37°C, chimeric mutant (Chim16) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1 (with an extra 22 amino acids substitution)

722632

3.2.1.21

3.6

-

pH 5.8, 37°C, mutant A375P

722632

3.2.1.21

3.7

-

pH 5.8, 37°C, mutant V196F/L203F

722632

3.2.1.21

6.52

-

pH 5.8, 37°C, mutant F469Y

722632

3.2.1.21

13.46

-

pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)

719801

3.2.1.21

14.3

-

pH 5.8, 37°C, wild-type

722632

3.2.1.21

18.68

-

pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)

719801

3.2.1.21

22.7

-

pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)

719801

3.2.1.21

23.41

-

pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)

719801

3.2.1.21

27.17

-

pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)

719801

3.2.1.21

31.83

-

pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)

719801

3.2.1.21

46.02

-

pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)

719801

3.2.1.21

53.96

-

pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)

719801

3.2.1.21

77.7

-

pH 5.8, 37°C, wild-type

719801

3.2.1.21

112.5

-

isoform GLU1, at pH 5.5 and 30°C

751824

3.2.1.21

22 entries

K_M Value (25 results)

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Show KM Value (25 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.2.1.182

4.8

-

recombinant enzyme, pH and temperature not specified in the publication

732629

3.2.1.21

0.031

-

pH 5.8, 37°C, mutant F205L

722632

3.2.1.21

0.04

-

pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)

719801

3.2.1.21

0.047

-

pH 5.8, 37°C, mutant Y473F

722632

3.2.1.21

0.05

-

pH 5.8, 37°C, wild-type

719801

3.2.1.21

0.058

-

pH 5.8, 37°C, mutant F198V/F205L/P377A

722632

3.2.1.21

0.06

-

pH 5.8, 37°C, mutant A375P

722632

3.2.1.21

0.061

-

pH 5.8, 37°C, wild-type

722632

3.2.1.21

0.065

-

pH 5.8, 37°C, mutant F466S/A467S

722632

3.2.1.21

0.065

-

pH 5.8, 37°C, mutant V196F/L203F

722632

3.2.1.21

0.066

-

pH 5.8, 37°C, mutant M263F

722632

3.2.1.21

0.076

-

pH 5.8, 37°C, chimeric mutant (Chim21) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1

722632

3.2.1.21

0.09

-

pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)

719801

3.2.1.21

0.092

-

pH 5.8, 37°C, mutant F466S

722632

3.2.1.21

0.1

-

pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)

719801

3.2.1.21

0.101

-

pH 5.8, 37°C, chimeric mutant (Chim16) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1 (with an extra 22 amino acids substitution)

722632

3.2.1.21

0.12

-

pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)

719801

3.2.1.21

0.127

-

pH 5.8, 37°C, mutant F469Y

722632

3.2.1.21

0.15

-

pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)

719801

3.2.1.21

0.18

-

pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)

719801

3.2.1.21

0.36

-

pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)

719801

3.2.1.21

0.4

-

beta-glucosidase C, pH 5, 30°C

723352

3.2.1.21

0.51

-

pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)

719801

3.2.1.21

1.9

-

isoform GLU1, at pH 5.5 and 30°C

751824

3.2.1.21

2

-

beta-glucosidase B, pH 5, 30°C

723352

3.2.1.21

24 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.2.1.182

0.0541

-

pH 5.5, 24°C

720757

References & Links

Literature References (13)

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Show Reference (13 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4892

16660850

Tissue distributions of dhurrin and of enzymes involved in its metabolism in leaves of Sorghum bicolor

1979

Kojima, M.; Poulton, J.E.; Thayer, S.S.; Conn, E.E.

Plant Physiol.

63

1022-1028

326271

10380623

Production and properties of the linamarase and amygdalase activities of Penicillium aurantiogriseum P35

1999

Petruccioli, M.; Brimer, L.; Cicalini, A.R.; Pulci, V.; Federici, F.

Biosci. Biotechnol. Biochem.

63

805-812

489458

4416442

The purification and properties of a uridine diphosphate glucose: aldehyde cyanohydrin beta-glucosyltransferase from sorghum seedlings

1974

Reay, P.F.; Conn, E.E.

J. Biol. Chem.

249

5826-5830

489460

16662753

Subcellular localization of a UDP-glucose:aldehyde cyanohydrin beta-glucosyl transferase in epidermal plastids of Sorghum leaf blades

1982

Surkin Wurtele, E.; Thayer, S.S.; Conn, E.E.

Plant Physiol.

70

1732-1737

489461

10585420

The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate specificity

1999

Jones, P.R.; Moller, B.L.; Hoj, P.B.

J. Biol. Chem.

274

35483-35491

665542

15148317

Structural determinants of substrate specificity in family 1 beta-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex with its natural substrate

2004

Verdoucq, L.; Moriniere, J.; Bevan, D.R.; Esen, A.; Vasella, A.; Henrissat, B.; Czjze, M.

J. Biol. Chem.

279

31796-31803

719801

10748038

The aglycone specificity-determining sites are different in 2, 4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA)-glucosidase (Maize beta -glucosidase) and dhurrinase (Sorghum beta -glucosidase)

2000

Cicek, M.; Blanchard, D.; Bevan, D.R.; Esen, A.

J. Biol. Chem.

275

20002-20011

720757

-

Substrate specificity of maize beta-glucosidase

1994

Babcock, G.; Esen, A.

Plant Sci.

101

31-39

720952

11106394

The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes

2000

Czjzek, M.; Cicek, M.; Zamboni, V.; Bevan, D.R.; Henrissat, B.; Esen, A.

Proc. Natl. Acad. Sci. USA

97

13555-13560

722632

12684498

Mutational and structural analysis of aglycone specificity in maize and sorghum beta-glucosidases

2003

Verdoucq, L.; Czjzek, M.; Moriniere, J.; Bevan, D.R.; Esen, A.

J. Biol. Chem.

278

25055-25062

723352

-

Characterization of cyanogenic glucosides and beta-glucosidases in Triglochin maritima seedlings

1979

Nahrstedt, A.; Hosel, W.; Walther, A.

Phytochemistry

18

1137-1141

732629

22415274

Comparative analysis of benzoxazinoid biosynthesis in monocots and dicots: independent recruitment of stabilization and activation functions

2012

Dick, R.; Rattei, T.; Haslbeck, M.; Schwab, W.; Gierl, A.; Frey, M.

Plant Cell

24

915-928

751824

30336442

A promiscuous beta-glucosidase is involved in benzoxazinoid deglycosylation in Lamium galeobdolon

2018

Hannemann, L.; Lucaciu, C.R.; Sharma, S.; Rattei, T.; Mayer, K.F.X.; Gierl, A.; Frey, M.

Phytochemistry

156

224-233

Links to other databases for Dhurrin

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Show Links (1 entry)

ChEBI

PubChem

-