Abstract:
:A pattern of allosteric control for aromatic biosynthesis in cyanobacteria relies upon early-pathway regulation as the major control point for the entire branched pathway. In Synechococcus sp. strain PCC6301 (Anacystis nidulans), two enzymes which form precursors for L-phenylalanine biosynthesis are subject to control by feedback inhibition. 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase (first pathway enzyme) is feedback inhibited by L-tyrosine, whereas prephenate dehydratase (enzyme step 9) is feedback inhibited by L-phenylalanine and allosterically activated by L-tyrosine. Mutants lacking feedback inhibition of prephenate dehydratase excreted relatively modest quantities of L-phenylalanine. In contrast, mutants deregulated in allosteric control of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase excreted large quantities of L-phenylalanine (in addition to even greater quantities of L-tyrosine). Clearly, in the latter mutants, the elevated levels of prephenate must overwhelm the inhibition of prephenate dehydratase by L-phenylalanine, an effect assisted by increased intracellular L-tyrosine, an allosteric activator. The results show that early-pathway flow regulated in vivo by 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase is the dominating influence upon metabolite flow-through to L-phenylalanine. L-Tyrosine biosynthesis exemplifies such early-pathway control even more simply, since 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase is the sole regulatory enzyme subject to end-product control by L-tyrosine.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Hall GC,Flick MB,Jensen RAdoi
10.1128/JB.153.1.423-428.1983subject
Has Abstractpub_date
1983-01-01 00:00:00pages
423-8issue
1eissn
0021-9193issn
1098-5530journal_volume
153pub_type
杂志文章abstract::In rod-shaped bacteria, certain proteins are specifically localized to the cell poles. The nature of the positional information that leads to the proper localization of these proteins is unclear. In a screen for factors required for the localization of the Shigella sp. actin assembly protein IcsA to the bacterial pole...
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pub_type: 杂志文章
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doi:10.1128/JB.134.2.555-561.1978
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.155.3.1434-1438.1983
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pub_type: 杂志文章
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更新日期:1991-02-01 00:00:00
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pub_type: 杂志文章
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更新日期:1986-06-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.100.1.377-382.1969
更新日期:1969-10-01 00:00:00
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journal_title:Journal of bacteriology
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doi:10.1128/JB.125.3.1172-1179.1976
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pub_type: 杂志文章
doi:10.1128/jb.178.5.1480-1483.1996
更新日期:1996-03-01 00:00:00
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pub_type: 杂志文章
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更新日期:2002-03-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.178.18.5543-5545.1996
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journal_title:Journal of bacteriology
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doi:10.1128/JB.153.3.1315-1321.1983
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更新日期:1973-04-01 00:00:00
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更新日期:1974-01-01 00:00:00
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更新日期:1995-11-01 00:00:00
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journal_title:Journal of bacteriology
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更新日期:2014-11-01 00:00:00
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journal_title:Journal of bacteriology
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更新日期:1993-08-01 00:00:00
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更新日期:1998-04-01 00:00:00