FACULTY OF SCIENCE

UNIVERSITI TUNKU ABDUL RAHMAN

BACHELOR OF SCIENCE (HONOURS) – BIOCHEMISTRY

YEAR 2, TRIMESTER 2

UDEE2134 – MICROBIOLOGY I

ASSIGNMENT: STYRENE OXIDE ISOMERASE

NAME: LIM WEY LOON

STUDENT ID: 2207600

Styrene Oxide Isomerase (SOI)

The nomenclature for SOI is EC 5.3.99.7 (McDonald, 2023). It is a protein with 169

amino acids in its sequence with a mass of 18101 Da (Uni Prot, n.d.). SOI is used in the

conversion of styrene oxide to phenylacetaldehyde without producing acetophenone as a by-

product. The reverse reaction is not catalysed by this enzyme due to a lack of releasing

groups (e.g. halogen).

Figure 1: The reaction catalysed by SOI

(Itoh et al., 1997)

The catalytic mechanism of this reaction starts with the protonation of the oxirane

oxygen, which then causes the formation of a benzyl cation intermediate. This intermediate

then forms an enol and undergoes keto-enol tautomerism to form phenylacetaldehyde.

Figure 2: Mechanism for the action of SOI

(Oelschlägel, Zimmerling and Tischler, 2018)

 The Michaelis constant for the enzyme, Km is 7.7×10-5 M which is considered low.

Hence, SOI has a high affinity towards styrene oxide. On the other hand, SOI is highly

specific and only catalyse the reactions involving styrene oxide but not other epoxides (Itoh

et al., 1997).

In terms of regulation, various compounds possess effects on the catalytic properties

of SOI. Sulfhydryl reagents like p-chloromercuribenzoic acid can inhibit the reaction.

Hydrazine and hydroxylammonium chloride also inhibit SOI by reacting with carboxyl

compounds (Itoh et al., 1997).

SOI is a cofactor-independent enzyme and is stable due to membrane localization. For

instance, SOI is stable at neutral and alkaline conditions, with the pH ranging from 7 to 10.

Under acidic conditions, styrene oxide is unstable, and the reaction would not take place.

However, the enzyme SOI functions optimally at 40℃ (100% activity). Membrane

localization can only protect the enzyme against a temperature of 50 ℃ for a brief period

(Itoh et al., 1997; Oelschlägel, Zimmerling and Tischler, 2018).

Figure 3: Membrane localization of SOI in Pseudomonas fluorescens

(Uni Prot, n.d.)

The usage of SOI is significant in styrene degradation, or the peripheral styrene

catabolism of bacteria. Styrene and its metabolites can cause negative effects on human

health. Gaseous styrene released from industries has a bad odour and high toxicity (Itoh et al,
1997; Mooney, Ward, and O’Connor, 2006). On the other hand, styrene oxide is a known

carcinogen in the human liver (Foureman et al., 1989).

References:

Foureman, G.L., Harris, C.R.A.I.G., Guengerich, F.P. and Bend, J.R., 1989. Stereoselectivity

of styrene oxidation in microsomes and in purified cytochrome P-450 enzymes from rat liver.

Journal of Pharmacology and Experimental Therapeutics, [e-journal] 248(2), pp.492-497.

Doi: 10.1128/aem.64.6.2032-2043.1998

Itoh, N., Hayashi, K., Okada, K., Ito, T. and Mizuguchi, N., 1997. Characterization of Styrene

Oxide Isomerase, a Key Enzyme of Styrene and Styrene Metabolism in Corynebacterium sp.

Biosci. Biotech. Biochem., [e-journal] 61(12), pp.2058-2062.

https://doi.org/10.1271/bbb.61.2058

McDonald, A., 2023. The Enzyme List: Class 5 – Isomerases. [online] Available at:

<https://www.enzyme-database.org/downloads/ec5.pdf> [Accessed 22 February 2024].

Mooney, A., Ward, P.G. and O’Connor, E.K., 2006. Microbial Degradation of Styrene:

Biochemistry, Molecular Genetics, and Perspectives for Biotechnological Applications. Appl

Microbiol Biotechnol, [e-journal] 72(1), pp.1-10. Doi: 10.1007/s00253-006-0443-1

Oelschlägel, M., Zimmerling, J. and Tischler, D., 2018. A Review: The Styrene Metabolizing

Cascade of Side-Chain Oxygenation as Biotechnological Basis to Gain Various Valuable

Compounds. Frontiers in Microbiology, [e-journal] 9, p.490. Doi: 10.3389/fmicb.2018.00490

Uni Prot, n.d. styC – Styrene-Oxide Isomerase – Pseudomonas fluorescens. [online] Available

at: <https://www.uniprot.org/uniprotkb/O06836/entry> [Accessed 23 February 2024].