Abstract:
:Retinal and its derivatives represent essential compounds in many biological systems. In animals, they are synthesized through a symmetrical cleavage of beta-carotene catalysed by a monooxygenase. Here, we demonstrate that the open reading frame sll1541 from the cyanobacterium Synechocystis sp. PCC 6803 encodes the first eubacterial, retinal synthesizing enzyme (Diox1) thus far reported. In contrast to enzymes from animals, Diox1 converts beta-apo-carotenals instead of beta-carotene into retinal in vitro. The identity of the enzymatic product was proven by HPLC, GC-MS and in a biological test. Investigations, of the stereospecifity showed that Diox1 cleaved only the all-trans form of beta-apo-8'-carotenal, yielding all-trans-retinal. However, Diox1 exhibited wide substrate specificity with respect to chain-lengths and functional end-groups. Although with divergent Km and Vmax values, the enzyme converted beta-apo-carotenals, (3R)-3-OH-beta-apo-carotenals as well as apo-lycopenals into retinal, (3R)-3-hydroxy-retinal and acycloretinal respectively. In addition, the alcohols of these substrates were cleaved to yield the corresponding retinal derivatives.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Ruch S,Beyer P,Ernst H,Al-Babili Sdoi
10.1111/j.1365-2958.2004.04460.xsubject
Has Abstractpub_date
2005-02-01 00:00:00pages
1015-24issue
4eissn
0950-382Xissn
1365-2958pii
MMI4460journal_volume
55pub_type
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