Reaction participants Show >> << Hide
- Name help_outline (R)-synephrine Identifier CHEBI:63694 Charge 1 Formula C9H14NO2 InChIKeyhelp_outline YRCWQPVGYLYSOX-VIFPVBQESA-O SMILEShelp_outline C[NH2+]C[C@H](O)c1ccc(O)cc1 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (4-hydroxyphenyl)acetaldehyde Identifier CHEBI:15621 (CAS: 7339-87-9) help_outline Charge 0 Formula C8H8O2 InChIKeyhelp_outline IPRPPFIAVHPVJH-UHFFFAOYSA-N SMILEShelp_outline [H]C(=O)Cc1ccc(O)cc1 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline methylamine Identifier CHEBI:59338 Charge 1 Formula CH6N InChIKeyhelp_outline BAVYZALUXZFZLV-UHFFFAOYSA-O SMILEShelp_outline C[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 29 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:32203 | RHEA:32204 | RHEA:32205 | RHEA:32206 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Purification and properties of synephrinase from Arthrobacter synephrinum.
Manne V., Kutty K.R., Pillarisetti S.R.
Synephrinase, an enzyme catalyzing the conversion of (-)-synephrine into p-hydroxyphenylacetaldehyde and methylamine, was purified to apparent homogeneity from the cell-free extracts of Arthrobacter synephrinum grown on (+/-)-synephrine as the sole source of carbon and nitrogen. A 40-fold purifica ... >> More
Synephrinase, an enzyme catalyzing the conversion of (-)-synephrine into p-hydroxyphenylacetaldehyde and methylamine, was purified to apparent homogeneity from the cell-free extracts of Arthrobacter synephrinum grown on (+/-)-synephrine as the sole source of carbon and nitrogen. A 40-fold purification was sufficient to produce synephrinase that is apparently homogeneous as judged by native polyacrylamide gel electrophoresis and has a specific activity of 1.8 mumol product formed/min/mg protein. Thus, the enzyme is a relatively abundant enzyme, perhaps comprising as much as 2.5% of the total protein. The enzyme essentially required a sulfhydryl compound for its activity. Metal ions like Mg2+, Ca2+, and Mn2+ stimulated the enzyme activity. Metal chelating agents, thiol reagents, denaturing agents, and metal ions like Zn2+, Hg2+, Ag1+, and Cu2+ inhibited synephrinase activity. Apart from (-)-synephrine, the enzyme acted upon (+/-)-octopamine and beta-methoxysynephrine. Molecular oxygen was not utilized during the course of the reaction. The molecular mass of the enzyme as determined by Sephadex G-200 chromatography, was around 156,000. The enzyme was made up of four identical subunits with a molecular mass of 42,000. << Less
Arch Biochem Biophys 248:324-334(1986) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Conversion of (+/-)-synephrine into p-hydroxyphenylacetaldehyde by Arthrobacter synephrinum. A novel enzymic reaction.
Veeraswamy M., Devi N.A., Kutty R.K., Rao P.V.
A partically purified enzyme from Arthrobacter synephrinum was found to catalyse the conversion of (+/-)-synphrine into p-hydroxyphrenylacetaldehyde and methylamine. The enzyme is highly specific for synephrine and is distinctly different from monoamine oxidase.
Biochem J 159:807-809(1976) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.