Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.14/143887
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- Title
- Mammalian forebrain ketimine reductase identified as μ-crystallin; potential regulation by thyroid hormones
- Related
- Journal of neurochemistry, Vol. 118, No. 3, (2011), p.379-387
- DOI
- 10.1111/j.1471-4159.2011.07220.x
- Publisher
- Wiley-Blackwell
- Date
- 2011
- Author/Creator
- Hallen, André
- Author/Creator
- Cooper, Arthur J. L
- Author/Creator
- Jamie, Joanne F
- Author/Creator
- Haynes, Paul A
- Author/Creator
- Willows, Robert D
- Description
- Ketimine reductase (E.C. 1.5.1.25) was purified to apparent homogeneity from lamb forebrain by means of a rapid multi-step chromatography protocol. The purified enzyme was identified by MS/MS (mass spectrometry) as μ-crystallin. The identity was confirmed by heterologously expressing human μ-crystallin in Escherichia coli and subsequent chromatographic purification of the protein. The purified human μ-crystallin was confirmed to have ketimine reductase activity with a maximum specific activity similar to that of native ovine ketimine reductase, and was found to catalyse a sequential reaction. The enzyme substrates are putative neuromodulator/transmitters. The thyroid hormone 3,5,3′-l-triiodothyronine (T3) was found to be a strong reversible competitive inhibitor, and may have a novel role in regulating their concentrations. μ-Crystallin is also involved in intracellular T3 storage and transport. This research is the first to demonstrate an enzyme function for μ-crystallin. This newly demonstrated enzymatic activity identifies a new role for thyroid hormones in regulating mammalian amino acid metabolism, and a possible reciprocal role of enzyme activity regulating bioavailability of intracellular T3.
- Description
- 9 page(s)
- Subject Keyword
- μ-crystallin
- Subject Keyword
- CRYM
- Subject Keyword
- ketimine
- Subject Keyword
- triiodothyronine
- Resource Type
- journal article
- Organisation
- Macquarie University. Dept. of Chemistry and Biomolecular Sciences
- Identifier
- http://hdl.handle.net/1959.14/143887
- Identifier
- ISSN:0022-3042
- Identifier
- mq_res-ext-2-s2.0-79960333004
- Language
- eng
- Reviewed
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