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Literature summary extracted from

  • Pazhang, M.; Mardi, N.; Mehrnejad, F.; Chaparzadeh, N.
    The combinatorial effects of osmolytes and alcohols on the stability of pyrazinamidase methanol affects the enzyme stability through hydrophobic interactions and hydrogen bonds (2018), Int. J. Biol. Macromol., 108, 1339-1347 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.B15 gene pncA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis

General Stability

EC Number General Stability Organism
3.5.1.B15 stability and structure of recombinant pyrazinamidase (PZase) from Mycobacterium tuberculosis in alcohols, i.e. methanol, ethanol, isopropanol and n-propanol, are analyzed in the presence of absence of stabilizing osmolytes, sorbitol, sucrose and glycerol, overview. Methanol destabilizes, while glacerol stabilizes the enzyme. A decrease in the tertiary structure of the enzyme is less in the presence of ethanol, compared to the solutions of other alcohols. These results indicate that methanol, isopropanol and n-propanol decrease the tertiary structure of PZase in a similar manner Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.B15 pyrazinamide + H2O Mycobacterium tuberculosis
-
 pyrazinoic acid + NH3
-
 ?
3.5.1.B15 pyrazinamide + H2O Mycobacterium tuberculosis H37Rv
-
 pyrazinoic acid + NH3
-
 ?
3.5.1.B15 pyrazinamide + H2O Mycobacterium tuberculosis ATCC 25618
-
 pyrazinoic acid + NH3
-
 ?

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.5.1.B15 Methanol can interact with PZase via hydrophobic interactions and hydrogen bonds resulting in destabilization of the structure of the enzyme. Glycerol probably increases the stability of the enzyme in methanol by disrupting the unfavorable hydrophobic interactions and hydrogen bonds Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.B15 Mycobacterium tuberculosis I6XD65
-
-
3.5.1.B15 Mycobacterium tuberculosis ATCC 25618 I6XD65
-
-
3.5.1.B15 Mycobacterium tuberculosis H37Rv I6XD65
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.B15 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.B15 pyrazinamide + H2O
-
 Mycobacterium tuberculosis pyrazinoic acid + NH3
-
 ?
3.5.1.B15 pyrazinamide + H2O
-
 Mycobacterium tuberculosis H37Rv pyrazinoic acid + NH3
-
 ?
3.5.1.B15 pyrazinamide + H2O
-
 Mycobacterium tuberculosis ATCC 25618 pyrazinoic acid + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.B15 PZAse
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.B15 37
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.B15 7.5
-
 assay at Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
3.5.1.B15 additional information stability and structure of recombinant pyrazinamidase (PZase) from Mycobacterium tuberculosis are analyzed in the presence of stabilizing osmolytes sorbitol, sucrose and glycerol, and alcohols methanol, ethanol, isopropanol and n-propanol, overview Mycobacterium tuberculosis