4.1.1.96: carboxynorspermidine decarboxylase
This is an abbreviated version!
For detailed information about carboxynorspermidine decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.96
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4.1.1.96
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polyamine
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putrescine
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vibrio
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s-adenosylmethionine
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schiff
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agrobacterium
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beta-semialdehyde
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microbiota
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polyamine-free
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tumefaciens
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pyridoxal
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sym-norspermidine
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cholerae
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decarboxylases
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ornithine
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1,3-diaminopropane
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alginolyticus
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5'-phosphate
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planktonic
- 4.1.1.96
- polyamine
- putrescine
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vibrio
- s-adenosylmethionine
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schiff
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agrobacterium
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beta-semialdehyde
- microbiota
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polyamine-free
- tumefaciens
- pyridoxal
- sym-norspermidine
- cholerae
- decarboxylases
- ornithine
- 1,3-diaminopropane
- alginolyticus
- 5'-phosphate
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planktonic
Reaction
Synonyms
Atu4169, BT_0674, C-NSPD decarboxylase, CANS DC, CANSDC, carboxyspermidine decarboxylase, CasDC, nspC, VC1623
ECTree
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General Information
General Information on EC 4.1.1.96 - carboxynorspermidine decarboxylase
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malfunction
metabolism
physiological function
exogenous spermidine and norspermidine restore prototrophic growth for DELTA(CASDH) carboxynorspermidine synthase and DELTA(CASDC) carboxynorspermidine decarboxylase mutants
malfunction
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exogenous spermidine and norspermidine restore prototrophic growth for DELTA(CASDH) carboxynorspermidine synthase and DELTA(CASDC) carboxynorspermidine decarboxylase mutants
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carboxynorspermidine decarboxylase is acting as the last enzyme in norspermidine biosynthesis
metabolism
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the CANSDH/CANSDC alternative polyamine biosynthetic pathway is able to synthesize both sym-norspermidine and spermidine
physiological function
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carboxynorspermidine decarboxylase (NspC) levels inversely regulate biofilm and motility and implicate the presence of an effective feedback mechanism maintaining norspermidine homeostasis in Vibrio cholerae. High levels of NspC enhances growth, biofilm formation with 5fold increase in biofilm cell density, and vps gene transcription and decreases motility. Increased NspC levels do not lead to increases in intracellular norspermidine production
physiological function
a deletion mutant shows severe growth defects in minimal medium and a severe biofilm deficiency. Exogenous spermidine and norspermidine restore prototrophic growth for CASDC mutants, but only spermidine inhibits biofilm formation. The CASDC mutants accumulate homospermidine via a homospermidine synthase homologue
physiological function
Deletion of the gene encoding carboxyspermidine decarboxylase results in the depletion of spermidine and loss of decarboxylase activity. The deletion strain also shows growth defects in polyamine-free growth medium
physiological function
identification of a spermidine retroconversion activity in bacteria, producing diamine putrescine from triamine spermidine. When spermidine levels are pharmacologically decreased, synthesis of spermine from spermidine is induced via carboxyspermidine dehydrogenase and carboxyspermidine decarboxylase which produce spermidine from putrescine. A strain lacking carboxyspermidine decarboxylase activity accumulates carboxyspermidine, some putrescine and a small amount of homospermidine
physiological function
Vibrio cholerae serotype O1 MO10
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carboxynorspermidine decarboxylase (NspC) levels inversely regulate biofilm and motility and implicate the presence of an effective feedback mechanism maintaining norspermidine homeostasis in Vibrio cholerae. High levels of NspC enhances growth, biofilm formation with 5fold increase in biofilm cell density, and vps gene transcription and decreases motility. Increased NspC levels do not lead to increases in intracellular norspermidine production
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physiological function
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Deletion of the gene encoding carboxyspermidine decarboxylase results in the depletion of spermidine and loss of decarboxylase activity. The deletion strain also shows growth defects in polyamine-free growth medium
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physiological function
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identification of a spermidine retroconversion activity in bacteria, producing diamine putrescine from triamine spermidine. When spermidine levels are pharmacologically decreased, synthesis of spermine from spermidine is induced via carboxyspermidine dehydrogenase and carboxyspermidine decarboxylase which produce spermidine from putrescine. A strain lacking carboxyspermidine decarboxylase activity accumulates carboxyspermidine, some putrescine and a small amount of homospermidine
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physiological function
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a deletion mutant shows severe growth defects in minimal medium and a severe biofilm deficiency. Exogenous spermidine and norspermidine restore prototrophic growth for CASDC mutants, but only spermidine inhibits biofilm formation. The CASDC mutants accumulate homospermidine via a homospermidine synthase homologue
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