Glutamyl Endopeptidase II

Stennicke, Henning R.

doi:10.1016/b978-0-12-382219-2.00566-4

Cited by 1 publication

(1 citation statement)

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“…zyme preferentially cleaves glutamic acid and proline at the P2 position. However, GluSGP activity decreases when proline or aspartic acid possesses the P¢1 position (Stennicke and Breddam, 2013). According to this information, it can be considered that proline at position P2 contributes to the cleavage of glutamic acid at the P1 position, whereas proline at position P¢1 decelerates the cleavage, consequently leading to the gradual increase in the activity of AglST1.…”

Section: Discussionmentioning

confidence: 99%

Enzymatic and molecular characterization of α-1,3-glucanase (AglST2) from <i>Streptomyces thermodiastaticus</i> HF3-3 and its relation with α-1,3-glucanase HF65 (AglST1)

Cherdvorapong

Fujiki

Suyotha

et al. 2019

J. Gen. Appl. Microbiol.

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Extracellular α-1,3-glucanase HF90 (AglST2), with a sodium dodecyl sulfate (SDS)-PAGE-estimated molecular mass of approximately 91 kDa, was homogenously purified from the culture filtrate of Streptomyces thermodiastaticus HF3-3. AglST2 showed a high homology with mycodextranase in an amino acid sequence and demonstrated specificity with an α-1,3-glycosidic linkage of homo α-1,3-glucan. It has been suggested that AglST2 may be a new type of α-1,3-glucanase. The optimum pH and temperature of AglST2 were pH 5.5 and 60°C, respectively. AglST2 action was significantly stimulated in the presence of 5-20% (w/v) NaCl, and 1 mM metal ions Mn and Co. On the other hand, it was inhibited by 1 mM of Ag, Cu, Fe and Ni. Regarding the stability properties, AglST2 retained more than 80% of its maximum activity over a pH range of 5.0-7.0 at up to 60°C and in the presence of 0-20% (w/v) NaCl. Based on these results, the properties of AglST2 were comparable with those of AglST1, which had been previously purified and characterized from S. thermodiastaticus HF3-3 previously. The N-terminal amino acid sequence of AglST2 showed a good agreement with that of AglST1, suggesting that AglST1 was generated from AglST2 by proteolysis during cultivation. MALDI-TOF mass analysis suggested that AglST1 might be generated from AglST2 by the proteolytic removal of C-terminus polypeptide (approximately 20 kDa). Our investigation thus revealed the properties of AglST2, such as tolerance against high temperature, salts, and surfactants, which have promising industrial applications.

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Section: Discussionmentioning

confidence: 99%