Information on EC 2.4.1.218 - hydroquinone glucosyltransferase

Substrates: substrate specificity of wild-type and E368A mutant enzymes, overview
Products: -

additional information

Substrates: substrate specificity of wild-type and E368A mutant enzymes, overview
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

UDP-glucose + hydroquinone

UDP + hydroquinone-O-beta-D-glucopyranoside

additional information

Substrates: because hydroquinone and arbutin seem not to be naturally occuring compounds in Rauvolfia plants or cell culture, the enzyme must have another substrate specificity
Products: -

UDP-glucose + hydroquinone

UDP + hydroquinone-O-beta-D-glucopyranoside

Substrates: -
Products: -

UDP-glucose + hydroquinone

UDP + hydroquinone-O-beta-D-glucopyranoside

Substrates: -
Products: -

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Mg2+

10 mM, increases the conversion rate to 168.3%

Ni2+

required, metalloenzyme

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

Ca2+

10 mM, 24.4% inhibition

Co2+

10 mM, 54.2% inhibition

dichlorophen

Hg2+

10 mM, complete inhibition, reversed by addition of 20 mM 2-mercaptoethanol

hydroquinone

Glu274 is acting as an acidic backbone acceptor residue. Lys262, a basic amino acid from the active site of wheat Hydroquinone glucosyltransferase interacts with the hydroxyl group of hydroquinone and behaves as a side chain donor molecule. Asp264 is also observed as an interacting residue from the active site of hydroquinone glucosyltransferase. It binds to the hydroxyl group of hydroquinone inhibitor and donates hydrogen ion from its side chain group

Mn2+

10 mM, 24.7% inhibition

N-(n-butyl) phosphorothiocic triamide

Glu274 is acting as an acidic backbone donor residue and interacts with the amino group of the inhibitor

phenyl phosphorodiamate

Glu395 is directly interacting with amino group of the inhibitor

Zn2+

10 mM, 87.4% inhibition

additional information

dichlorophen

dichlorophen

additional information

enzyme molecular docking of urease inhibitors hydroquinone, phenyl phosphorodiamate, and N-(n-butyl) phosphorothiocic triamide, three-dimensional structure analysis using homology modeling, and interactions analysis, overview

additional information

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.43

hydroquinone

pH 7.5, 30°C

1.1

TDPglucose

0.077

UDPglucose

0.55

umbelliferone

0.398 - 0.706

Vanillin

6 entries

additional information

3 entries

0.398

Vanillin

pH 7.5, 50°C, recombinant mutant E368A

0.411

Vanillin

pH 7.5, 50°C, recombinant mutant E368D

0.44

Vanillin

0.44

Vanillin

pH 7.5, 50°C, recombinant wild-type enzyme

0.452

Vanillin

pH 7.5, 50°C, recombinant mutant L86I

0.706

Vanillin

pH 7.5, 50°C, recombinant mutant A204V

additional information

Km value for hydroquinone is below 0.001 mM

additional information

Km value for hydroquinone is below 0.001 mM

additional information

Km value for hydroquinone is below 0.001 mM

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.00038

hydroquinone

pH 7.5, 30°C

0.08 - 2.59

Vanillin

5 entries

0.08

Vanillin

pH 7.5, 50°C, recombinant mutant E368A

0.12

Vanillin

pH 7.5, 50°C, recombinant mutant E368D

1.3

Vanillin

pH 7.5, 50°C, recombinant mutant A204V

1.84

Vanillin

pH 7.5, 50°C, recombinant mutant L86I

2.59

Vanillin

pH 7.5, 50°C, recombinant wild-type enzyme

show all columns Go to kcat/KM Value Search

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.0009

hydroquinone

pH 7.5, 30°C

show all columns Go to Ki Value Search

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.00009

dichlorophen

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.003

purified recombinant mutant H360E, substrate hydroquinone

0.01

purified recombinant mutant H360K, substrate hydroquinone

0.013

purified recombinant mutant H360R, substrate hydroquinone

0.054

purified recombinant mutant E368D, substrate vanillin

0.066

purified recombinant mutant E368A, substrate vanillin

0.79

purified recombinant mutant A204V, substrate vanillin

1.07

purified recombinant mutant E368D, substrate hydroquinone

1.22

purified recombinant mutant L86I, substrate vanillin

1.44

purified recombinant mutant E368A, substrate hydroquinone

1.45

purified recombinant wild-type enzyme, substrate vanillin

10.82

purified recombinant mutant L86I, substrate hydroquinone

12.17

purified recombinant wild-type enzyme, substrate hydroquinone

8.34

purified recombinant mutant A204V, substrate hydroquinone

additional information

3 entries

additional information

additional information

substrate specificity of wild-type and E368A mutant enzymes, overview

additional information

substrate specificity of wild-type and E368A mutant enzymes, overview

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4.5

and a second optimum at pH 6.8 in phosphate buffer, and a second optimum at pH 7.5 in citric acid buffer

6.8

show all columns Go to Temperature Optimum Search

and a second optimum at pH 4.5, phosphate buffer

7.5

7.5

and a second optimum at pH 4.5, citric acid buffer

7.5

assay at

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

recombinant enzyme

assay at

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

UniProt

brenda

brenda

SwissProt

brenda

brenda

658631, 745691, 764953

SwissProt

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

cell culture

cell suspension culture

brenda

brenda

brenda

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

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).

Q9AR73 pBLAST

HQGT_RAUSE

470

51794

Swiss-Prot

Show Sequence

D8LAL9 pBLAST

D8LAL9_WHEAT

493

52450

TrEMBL

Show Sequence

Q9M156 pBLAST

U72B1_ARATH

Arabidopsis thaliana

480

52930

Swiss-Prot

Show Sequence

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

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

51800

show all columns Go to Subunit Search

x * 51800, calculation from nucleotide sequence

52000

x * 52000, SDS-PAGE

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

show all columns Go to Protein Variants Search

x * 51800, calculation from nucleotide sequence

x * 52000, SDS-PAGE

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

A204V

site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme

E368A

site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme

E368D

site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme

H360E

site-directed mutagenesis, mutant shows about 4000fold reduced activity compared to the wild-type enzyme

H360K

site-directed mutagenesis, mutant shows about 1000fold reduced activity compared to the wild-type enzyme

H360R

site-directed mutagenesis, mutant shows about 1000fold reduced activity compared to the wild-type enzyme

L86I

site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme

additional information

additional information

generation of the typical E-E motif of the enzyme does not convert a NRD1beta enzyme into a NRD1alpha enzyme

additional information

generation of the typical E-E motif of the enzyme does not convert a NRD1beta enzyme into a NRD1alpha enzyme

show all columns Go to Temperature Stability Search

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

1 h, stable

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

Go to Cloned (commentary) Search

recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

cDNA with 6xHis tag

DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain M15

expression in Escherichia coli

expression in Escherichia coli

show all columns Go to Application Search

expression in Escherichia coli

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

synthesis

3 entries

synthesis

formation of arbutin, which is a potent inhibitor of human melanin biosynthesis with commercial value

synthesis

an artificial pathway is established in Escherichia coli for high-level production of arbutin from simple carbon sources in Escherichia coli for high-level production of arbutin from simple carbon sources. Introduction of the genes for 4-hydroxybenzoate 1-hydroxylase from Candida parapsilosis CBS604 and hydroquinone glucosyltransferase from Rauvolfia serpentina into Escherichia coli leads to the production of 54.71 mg/l of arbutin from glucose. Further redirection of carbon flux into arbutin biosynthesis pathway by enhancing shikimate pathway genes enables production of 3.29 g/l arbutin. Final optimization of glucose concentration added in the culture medium is able to further improve the titer of arbutin to 4.19 g/l in shake flasks experiments

synthesis

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production of arbutin in Yarrowia lipolytica by codon-optimized expression of chorismate pyruvate-lyase (UbiC), 4-hydroxybenzoate 1-hydroxylase (MNX1), and hydroquinone glucosyltransferase (AS) with overexpression of seven arbutin-biosynthesis molecular targets. Through optimization, a maximum arbutin titer of 8.6 g/l is achieved

764953

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Arend, J.; Warzecha, H.; St�ckigt, J.

Hydroquinone:O-glucosyltransferase from cultivated Rauvolfia cells: enrichment and partial amino acid sequences

Phytochemistry

187-193

2000

Rauvolfia serpentina

10680170

brenda

Hefner, T.; Arend, J.; Warzecha, H.; Siems, K.; St�ckigt, J.

Arbutin synthase, a novel member of the NRD1beta glycosyltransferase family, is a unique multifunctional enzyme converting various natural products and xenobiotics

Bioorg. Med. Chem.

1731-1741

2002

Rauvolfia serpentina (Q9AR73), Rauvolfia serpentina

11937332

brenda

Arend, J.; Warzecha, H.; Hefner, T.; St�ckigt, J.

Utilizing genetically engineered bacteria to produce plant-specific glucosides

Biotechnol. Bioeng.

126-131

2001

Rauvolfia serpentina

11505382

brenda

Hefner, T.; Stockigt, J.

Probing suggested catalytic domains of glycosyltransferases by site-directed mutagenesis

Eur. J. Biochem.

270

533-538

2003

Rauvolfia serpentina (Q9AR73), Rauvolfia serpentina

12542702

brenda

Huma, T.; Maryam, A.; Qamar, T.U.

Molecular modeling and docking of wheat hydroquinone glucosyl transferase by using hydroquinone, phenyl phosphorodiamate and n-(n butyl) phosphorothiocic triamide as inhibitors

Bioinformation

124-129

2014

Triticum aestivum (D8LAL9), Triticum aestivum

24748751

brenda