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Literature summary for 1.2.1.9 extracted from

  • Arutyunov, D.; Schmalhausen, E.; Orlov, V.; Rahuel-Clermont, S.; Nagradova, N.; Branlant, G.; Muronetz, V.
    An unusual effect of NADP+ on the thermostability of the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (2013), Biochem. Cell Biol., 91, 295-302 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Streptococcus mutans
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Subunits

Subunits Comment Organism
tetramer
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Streptococcus mutans

Synonyms

Synonyms Comment Organism
GAPN
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Streptococcus mutans
nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
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Streptococcus mutans

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
additional information
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effect of NADP+ on the thermostability and the irreversible thermal denaturation of the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. The enzyme-NADP+ binary complex shows a strongly decreased thermal stability, with a difference of about 20┬░C between the temperatures of the thermal transition peak maxima of the complex and the free protein. GAPN thermal inactivation is considerably decelerated in the presence of NADP+ showing that the apparent change in stability of the active centre can be the opposite to that of the whole protein molecule. NADP+ can also reactivate the inactive GAPN species, obtained by heating of the apoenzyme below the thermal denaturation transition temperature. The mechanism provides GAPN the sufficient flexibility for the earlier observed profound active site reorganizations required during the catalytic cycle. The elevated thermal stability of the apoenzyme may, in turn, be important for maintaining a constant level of active GAPN Streptococcus mutans

Cofactor

Cofactor Comment Organism Structure
NADP+ effect of NADP+ on the thermostability and the irreversible thermal denaturation of the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. The enzyme-NADP+ binary complex shows a strongly decreased thermal stability, with a difference of about 20┬░C between the temperatures of the thermal transition peak maxima of the complex and the free protein. Single amino acid substitution, known to abolish the NADP+ binding, cancelled the calorimetric effect of the coenzyme Streptococcus mutans

General Information

General Information Comment Organism
malfunction single amino acid substitution, known to abolish the NADP+ binding, cancelled the calorimetric effect of the coenzyme NADP+ Streptococcus mutans
physiological function the enzyme is known to be crucial for the effective supply of the reducing equivalents in Streptococcus mutans and its ability to grow under aerobic conditions Streptococcus mutans