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Literature summary for 2.4.1.1 extracted from

  • Schwarz, A.; Brecker, L.; Nidetzky, B.
    Probing the active site of Corynebacterium callunae starch phosphorylase through the characterization of wild-type and His334-->Gly mutant enzymes (2007), FEBS J., 274, 5105-5115.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
imidazole stimulates activity of the mutant up to 5.5fold Corynebacterium callunae

Protein Variants

Protein Variants Comment Organism
H334G purified H334G shows 0.05% and 1.3% of wild-type catalytic center activity for phosphorolysis of maltopentaose and substrate binding affinity in the ternary complex with enzyme bound to phosphate, respectively. Disruption of enzyme-substrate interactions in H334G is strictly local, affecting the protein environment of sugar carbon 6. pH profiles of the phosphorolysis rate for wild-type and H334G are both bell-shaped, with the broad pH range of optimum activity in the wild-type (pH 6.5-7.5) being narrowed and markedly shifted to lower pH values in the mutant (pH 6.5-7.0). External imidazole partly restores the activity lost in the mutant, without participating as an alternative nucleophile in the reaction Corynebacterium callunae

Inhibitors

Inhibitors Comment Organism Structure
2-ethylimidazole weak inhibition of wild-type activity, inhibition of mutant enzyme H334G Corynebacterium callunae
2-methylimidazole weak inhibition of wild-type activity Corynebacterium callunae
acetate weak inhibition of wild-type activity, no effect on the activity of the H334G mutant Corynebacterium callunae
azide weak inhibition of wild-type activity Corynebacterium callunae
formate 5fold reduction of wild-type activity, no effect on the activity of the H334G mutant Corynebacterium callunae
imidazole weak inhibition of wild-type enzyme Corynebacterium callunae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
280
-
 maltopentaose pH 7.0 Corynebacterium callunae

Organism

Organism UniProt Comment Textmining
Corynebacterium callunae Q8KQ56
-
-

Purification (Commentary)

Purification (Comment) Organism
Wild-type and the H334G mutant enzyme produced in Escherichia coli Corynebacterium callunae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltopentaose + phosphate
-
 Corynebacterium callunae ?
-
 ?

Synonyms

Synonyms Comment Organism
CcStP
-
 Corynebacterium callunae
starch phosphorylase
-
 Corynebacterium callunae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.033
-
 maltopentaose pH 7.0 Corynebacterium callunae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7.5 phosphorolysis of maltopdextrin, wild-type enzyme Corynebacterium callunae
6.5 7 phosphorolysis of maltopdextrin, mutant enzyme H334G Corynebacterium callunae

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate the 31P chemical shift of pyridoxal 5'-phosphate in the wild-type was pH-dependent and not perturbed by binding of arsenate. At pH 7.25, it is not sensitive to the replacement His334 by Gly Corynebacterium callunae