Information on EC 5.3.99.7 - styrene-oxide isomerase

Substrates: -
Products: -

styrene oxide + H2O

phenylacetaldehyde

Substrates: enzyme is involved in the pathway of styrene degradation
Products: -

styrene oxide + H2O

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide + H2O

phenylacetaldehyde

Substrates: styrene, styrene oxide, and phenylacetaldehyde induce the enzymes involved in the degradation of styrene to phenylacetic acid, glucose has no effect
Products: -

styrene oxide + H2O

phenylacetaldehyde

Xanthobacter sp.

Substrates: equilibrium constant favors phenylacetaldehyde formation
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

styrene oxide

phenylacetaldehyde

28 entries

styrene oxide + H2O

phenylacetaldehyde

7 entries

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Escherichia coli

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

768297, 768425, 774875, 771551

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

O50216

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Rhodococcus sp. (in: high G+C Gram-positive bacteria) ST-5

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Sphingobium sp. Kp5.1_1

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Sphingobium sp. Kp8.3_1b

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide

phenylacetaldehyde

Substrates: -
Products: -

styrene oxide + H2O

phenylacetaldehyde

aerobic bacterium (strain S5)

390293

Substrates: enzyme is involved in the pathway of styrene degradation
Products: -

styrene oxide + H2O

phenylacetaldehyde

648823

Substrates: -
Products: -

styrene oxide + H2O

phenylacetaldehyde

Substrates: key enzyme of styrene and styrene oxide metabolism
Products: -

styrene oxide + H2O

phenylacetaldehyde

Substrates: enzyme is involved in the pathway of styrene degradation
Products: -

styrene oxide + H2O

phenylacetaldehyde

Substrates: styrene, styrene oxide, and phenylacetaldehyde induce the enzymes involved in the degradation of styrene to phenylacetic acid, glucose has no effect
Products: -

styrene oxide + H2O

phenylacetaldehyde

Substrates: enzyme is involved in the pathway of styrene degradation
Products: -

styrene oxide + H2O

phenylacetaldehyde

Substrates: styrene, styrene oxide, and phenylacetaldehyde induce the enzymes involved in the degradation of styrene to phenylacetic acid, glucose has no effect
Products: -

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

additional information

7 entries

additional information

without need for any cofactor

additional information

cofactor-independent

additional information

cofactor-independent

additional information

cofactor-independent

additional information

cofactor-independent

additional information

cofactor-independent

additional information

cofactor-independent

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

non-metal enzyme

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

AgNO3

Show Disease (141 entries)

0.1 mM, 29% inhibition

dithiothreitol

1 mM, 22% inhibition

HgCl2

1 mM, 80% inhibition

hydrazine

1 mM, 82% inhibition

hydroxylammonium chloride

1 mM, 77% inhibition

iodoacetate

1 mM, 80% inhibition

KCN

1 mM, 32% inhibition

PCMB

1 mM, 24% inhibition

phenylacetaldehyde

irreversible product inhibition, half-life of 15 min determined at a phenylacetaldehyde concentration of about 55 mM

Tris hydrochloride

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.077

styrene oxide

pH 7.0, 25°C

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

150

after 2fold purification, at pH 7.2 and 37°C

32.2

crude cell extract, at pH 7.2 and 37°C

4.1

crude cell extract, at pH 7.2 and 37°C

42.1

partially purified enzyme, pH 7.2, 22°C

5.12

styrene-grown cell extract, pH 7.2, 22°C

58.7

6.035

75.9

crude cell extract, at pH 7.2 and 37°C

89.7

after 2.8fold purification, at pH 7.2 and 37°C

9.79

after 2.4fold purification, at pH 7.2 and 37°C

91.7

partially purified enzyme, pH 7.2, 65°C

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 - 7.5

6 - 8

show all columns Go to pH Range Search

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 - 10

pH 5.0-7.5: maximal activity, pH 10.0: about 50% of maximal activity

additional information

wide pH tolerance

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

show all columns Go to Temperature Range Search

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TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

20 - 70

activity range, wide temperature tolerance, profile overview

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

aerobic bacterium (strain S5)

390293

brenda

brenda

Escherichia coli

brenda

no activity in Gordonia rubripertincta DSM 46758

768719, 771551

brenda

no activity in Rhodococcus sp. ST-10

728003, 771551

brenda

390301, 648824, 679545, 682894, 768297, 768425, 771551, 774875

brenda

390301, 648824, 771551

brenda

682894, 774875

brenda

Pseudomonas putida SN1

brenda

brenda

brenda

3 entries

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

3 entries

gene styC, strain ST-5 has a gene cluster containing four open reading frames which encode styrene degradation enzymes

UniProt

brenda

Rhodococcus sp. (in: high G+C Gram-positive bacteria) ST-5

gene styC, strain ST-5 has a gene cluster containing four open reading frames which encode styrene degradation enzymes

UniProt

brenda

brenda

brenda

Sphingobium sp. Kp5.1_1

brenda

Sphingobium sp. Kp8.3_1b

brenda

Xanthobacter sp.

brenda

brenda

brenda

strain AC-5 and strain ST-5. Strain ST-10 does not have a styrene oxide isoemrase and metabolized styrene oxide by an unknown enzymatic reaction

648823

brenda

UniProt

brenda

brenda

UniProt

brenda

brenda

brenda

O50216

UniProt

brenda

brenda

UniProt

brenda

brenda

brenda

UniProt

brenda

brenda

UniProt

brenda

brenda

UniProt

brenda

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

cells grown in a styrene gas atmosphere

brenda

show all columns Go to Localization Search

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

20 entries

additional information

not membrane-bound, probably bound to the cell wall

brenda

brenda

integral membrane protein

brenda

brenda

brenda

brenda

brenda

brenda

O50216

integral membrane protein

brenda

brenda

integral membrane protein

brenda

brenda

integral membrane protein

brenda

brenda

brenda

brenda

Sphingobium sp. Kp5.1_1

brenda

Sphingobium sp. Kp8.3_1b

brenda

brenda

brenda

brenda

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Highest Expressing Human Cell Lines

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show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

metabolism

4 entries

additional information

metabolism

the enzyme is part of the upper pathway of styrene degradation via side chain oxygenation

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

metabolism

the enzyme is involved in the styrene degradation pathway, overview

metabolism

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

the enzyme is part of the upper pathway of styrene degradation via side chain oxygenation

metabolism

Rhodococcus sp. (in: high G+C Gram-positive bacteria) ST-5

the enzyme is involved in the styrene degradation pathway, overview

additional information

in strain ST-10, which lacks a styrene oxide isomerase, styrene oxide is converted to phenylacetaldehyde by spontaneous chemical reaction. The strain accumulates styrene oxide as a metabolic intermediate. The produced phenylacetaldehyde is converted to phenylacetic acid in strain ST-10 as well as in strain ST-5

additional information

Rhodococcus sp. (in: high G+C Gram-positive bacteria) ST-5

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).

O06836 pBLAST

STYC_PSEFL

169

18101

Swiss-Prot

A0A076JZU4 pBLAST

A0A076JZU4_RHOOP

168

18055

TrEMBL

A0A076K0M9 pBLAST

A0A076K0M9_9SPHN

186

20250

TrEMBL

G3XEX7 pBLAST

G3XEX7_9NOCA

168

18225

TrEMBL

Mitochondrion (Reliability: 2)

O50216 pBLAST

O50216_9PSED

169

18047

TrEMBL

Secretory Pathway (Reliability: 1)

show all columns Go to Subunit Search

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

6 entries

Escherichia coli

x * about 20000, calculated from amino acid sequence

x * 18000, calculated from amino acid sequence

x * 18000, calculated from amino acid sequence

x * 18000, calculated from amino acid sequence

x * 20000, calculated from amino acid sequence

x * 20000, calculated from amino acid sequence

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

additional information

679545

additional information

Pseudomonas putida SN1

show all columns Go to pH Stability Search

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

25°C, 1 h, 10% loss of activity

25°C, 1 h, unstable below

show all columns Go to Temperature Stability Search

partially purified native enzyme, 30 min, most stable at

7 - 8

25°C, 1 h

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

30 - 40

partially purified native enzyme, 30 min, most stable at

pH 7.0, 1 h, stable

pH 7.0, 1 h, 10% loss of activity

pH 7.0, 1 h, 50% loss of activity

pH 7.0, 1 h, 80% loss of activity

partially purified native enzyme, 30 min, inactivation

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

4°C, 50 mM potassium phosphate buffer, pH 7.0, 30% loss of activity after 2 weeks

Xanthobacter sp.

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

HisTrap column chromatography

native enzyme partially from styrene-grown cells by membrane preparation and solubilization

partial

partial purification

partial purification

partial purification

partial purification

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Escherichia coli

expressed in Escherichia coli BL21(DE3) cells

5 entries

expressed in Escherichia coli MG1655 (DE3) cells

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

768297

gene styC, DNA and amino acid sequence determination and analysis, genetic organization, expression in Escherichia coli

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells

Go to Expression Search

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

the enzyme is strongly induced by styrene, to a lesser extent by styrene oxide and phenylacetaldehyde, no induction by phenylacetic acid or glucose

the enzyme is strongly induced by styrene, to a lesser extent by styrene oxide and phenylacetaldehyde, no induction by phenylacetic acid or glucose

the enzyme is strongly induced by styrene, to a lesser extent by styrene oxide and phenylacetaldehyde, no induction by phenylacetic acid or glucose

show all columns Go to Application Search

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

synthesis

17 entries

synthesis

the highly stereospecific enzyme can be used in a biotransformation system producing (R)-styrene oxide

synthesis

enzyme disruption mutant is unable to grow on styrene or styrene oxide and accumulates enantiopure (S)-styrene when incubated with styrene. Upon growth on citrate as carbon source, mutant strain exhibits a high whole-cell activity of styrene oxide formation. In a 3 l bioreactor experiment, mutant can accumulate 150 mM (S)-styrene oxide at an enantiomerixc excess above 98% in 13 h

679545

synthesis

the enzyme can be used for tyrosol production as part of an enzyme cascade in recombinant Escherichia coli

768297

synthesis

the enzyme can be used in cascade biocatalysis for the production of acids amines, and alcohols. The enzyme is also involved in metabolic engineering for the production of 2-phenylethanol from renewable feedstock

synthesis

synthesis

synthesis

synthesis

synthesis

synthesis

Sphingobium sp. Kp5.1_1

synthesis

Sphingobium sp. Kp8.3_1b

synthesis

synthesis

synthesis

synthesis

synthesis

Pseudomonas putida SN1

synthesis

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

390293

Hartmans, S.; van der Werf, M.J.; de Bont, J.A.M.

Bacterial degradation of styrene involving a novel flavin adenine dinucleotide-dependent styrene monooxygenase

Appl. Environ. Microbiol.

1347-1351

1990

aerobic bacterium (strain S5)

2339888

brenda

Hartmans, S.; Smits, J.P.; van der Werf, M.J.; Volkering, F.; de Bont, J.A.M.

Metabolism of styrene oxide and 2-phenylethanol in the styrene-degrading Xanthobacter strain 124X

Appl. Environ. Microbiol.

2850-2855

1989

Xanthobacter sp.

16348047

brenda

O'Connor, K.; Duetz, W.; Wind, B.; Dobson, A.D.W.

The effect of nutrient limitation on styrene metabolism in Pseudomonas putida CA-3

Appl. Environ. Microbiol.

3594-3599

1996

Pseudomonas putida, Pseudomonas putida CA-3

8967774

brenda

648823

Itoh, N.; Yoshida, K.; Okada, K.

Isolation and identification of styrene-degrading Corynebacterium strains, and their styrene metabolism

Biosci. Biotechnol. Biochem.

1826-1830

1996

Corynebacterium sp.

8987859

brenda

O'Connor, K.; Buckley, C.M.; Hartmans, S.; Dobson, A.D.W.

Possible regulatory role for nonaromatic carbon sources in styrene degradation by Pseudomonas putida CA-3

Appl. Environ. Microbiol.

544-548

1995

Pseudomonas putida, Pseudomonas putida CA-3

7574594

brenda

Itoh, N.; Hayashi, K.; Okada, K.; Ito, T.; Mizuguchi, N.

Characterization of styrene oxide isomerase, a key enzyme of styrene and styrene oxide metabolism in Corynebacterium sp

Biosci. Biotechnol. Biochem.

2058-2062

1997

Corynebacterium sp., Pseudomonas sp., Pseudomonas sp. SK3

brenda

679545

Han, J.H.; Park, M.S.; Bae, J.W.; Lee, E.Y.; Yoon, Y.J.; Lee, S.; Park, S.

Production of (S)-styrene oxide using styrene oxide isomerase negative mutant of Pseudomonas putida SN1

Enzyme Microb. Technol.

1264-1269

2006

Pseudomonas putida, Pseudomonas putida SN1

brenda

682894

Miyamoto, K.; Okuro, K.; Ohta, H.

Substrate specificity and reaction mechanism of recombinant styrene oxide isomerase from Pseudomonas putida S12

Tetrahedron Lett.

3255-3257

2007

Pseudomonas putida, Pseudomonas putida S12

brenda

Oelschlaegel, M.; Groening, J.A.; Tischler, D.; Kaschabek, S.R.; Schloemann, M.

Styrene oxide isomerase of Rhodococcus opacus 1CP, a highly stable and considerably active enzyme

Appl. Environ. Microbiol.

4330-4337

2012

Rhodococcus opacus, Rhodococcus opacus 1CP

22504818

brenda

Toda, H.; Itoh, N.

Isolation and characterization of styrene metabolism genes from styrene-assimilating soil bacteria Rhodococcus sp. ST-5 and ST-10

J. Biosci. Bioeng.

113

12-19

2012

Rhodococcus sp. (in: high G+C Gram-positive bacteria) (G3XEX7), no activity in Rhodococcus sp. ST-10, Rhodococcus sp. (in: high G+C Gram-positive bacteria) ST-5 (G3XEX7)

21996027

brenda

Oelschlaegel, M.; Richter, L.; Stuhr, A.; Hofmann, S.; Schloemann, M.

Heterologous production of different styrene oxide isomerases for the highly efficient synthesis of phenylacetaldehyde

J. Biotechnol.

252

43-49

2017

Pseudomonas fluorescens (O06836), Rhodococcus opacus (A0A076JZU4), Sphingopyxis fribergensis (A0A076K0M9), Sphingopyxis fribergensis, Pseudomonas fluorescens ST (O06836), Pseudomonas fluorescens ST, Rhodococcus opacus 1CP (A0A076JZU4), Rhodococcus opacus 1CP, Sphingopyxis fribergensis Kp5.2 (A0A076K0M9)

28472670

brenda

768297

Lai, Y.; Chen, H.; Liu, L.; Fu, B.; Wu, P.; Li, W.; Hu, J.; Yuan, J.

Engineering a synthetic pathway for tyrosol synthesis in Escherichia coli

ACS Synth. Biol.

441-447

2022

Pseudomonas putida

34985865

brenda

See, W.; Li, X.; Li, Z.

Biocatalytic cascade conversion of racemic epoxides to (S)-2-arylpropionic acids, (R)- and (S)-2-arylpropyl amines

Adv. Synth. Catal.

365

68-77

2022

Pseudomonas putida

brenda

Xin, R.; See, W.W.L.; Yun, H.; Li, X.; Li, Z.

Enzyme-catalyzed Meinwald rearrangement with an unusual regioselective and stereospecific 1,2-methyl shift

Angew. Chem. Int. Ed. Engl.

e202204889

2022

Escherichia coli

35535736

brenda

768719

Heine, T.; Zimmerling, J.; Ballmann, A.; Kleeberg, S.B.; Rueckert, C.; Busche, T.; Winkler, A.; Kalinowski, J.; Poetsch, A.; Scholtissek, A.; Oelschlaegel, M.; Schmidt, G.; Tischler, D.

On the enigma of glutathione-dependent styrene degradation in Gordonia rubripertincta CWB2

Appl. Environ. Microbiol.

e00154-18

2018

no activity in Gordonia rubripertincta DSM 46758

29475871

brenda

Oelschlaegel, M.; Zimmerling, J.; Tischler, D.

A review The styrene metabolizing cascade of side-chain oxygenation as biotechnological basis to gain various valuable compounds

Front. Microbiol.

490

2018

no activity in Gordonia rubripertincta DSM 46758, no activity in Rhodococcus sp. ST-10, Pseudomonas putida, Rhodococcus sp. ST-5, Sphingopyxis fribergensis, Pseudomonas fluorescens, Rhodococcus opacus, Pseudomonas sp. VLB120, Pseudomonas fluorescens ST, Pseudomonas putida CA-3, Rhodococcus opacus 1CP, Sphingopyxis fribergensis Kp5.2

29623070

brenda

Choo, J.; Li, Z.

Styrene oxide isomerase catalyzed Meinwald rearrangement reaction discovery and application in single-step and one-pot cascade reactions

Org. Process Res. Dev.

1960-1970

2022

Corynebacterium sp. AC-5, Pseudomonas putida, Pseudomonas sp. VLB120, Pseudomonas fluorescens, Rhodococcus sp. 5.3_2_1, Rhodococcus opacus, Sphingobium sp. Kp5.1_1, Sphingobium sp. Kp8.3_1b, Sphingopyxis fribergensis, Xanthobacter sp. 124X, Pseudomonas fluorescens ST, Pseudomonas putida S12, Rhodococcus opacus 1CP

brenda