Literature summary for 3.5.1.B15 extracted from

Rasool, N.; Husssain, W.; Khan, Y.D.
Revelation of enzyme activity of mutant pyrazinamidases from Mycobacterium tuberculosis upon binding with various metals using quantum mechanical approach (2019), Comput. Biol. Chem., 83, 107108 .

Search for more literature for 3.5.1.B15

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of enzyme crystal structure, PDB ID 3PL1	Mycobacterium tuberculosis

Protein Variants

Protein Variants	Comment	Organism
D12A	site-directed mutagenesis, the mutation highly reduces the mutant activity compared to wild-type	Mycobacterium tuberculosis
D12G	site-directed mutagenesis, the mutation highly reduces the mutant activity compared to wild-type	Mycobacterium tuberculosis
D136G	site-directed mutagenesis, the mutation highly reduces the mutant activity compared to wild-type	Mycobacterium tuberculosis
D49N	site-directed mutagenesis, the mutation highly reduces the mutant activity compared to wild-type and has a deleterious effect on the metal binding mechanism of PZase	Mycobacterium tuberculosis
G78C	site-directed mutagenesis, the mutation highly reduces the mutant activity compared to wild-type and has a deleterious effect on the metal binding mechanism of PZase	Mycobacterium tuberculosis
H51R	site-directed mutagenesis, the mutation highly reduces the mutant activity compared to wild-type and has a deleterious effect on the metal binding mechanism of PZase	Mycobacterium tuberculosis
additional information	cumulative effect of mutations and iron substitution	Mycobacterium tuberculosis
T135P	site-directed mutagenesis, the mutation highly reduces the mutant activity compared to wild-type	Mycobacterium tuberculosis

Inhibitors

Inhibitors	Comment	Organism	Structure
Cu2+	-	Mycobacterium tuberculosis
Mg2+	-	Mycobacterium tuberculosis
Zn2+	-	Mycobacterium tuberculosis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	activates	Mycobacterium tuberculosis
Fe2+	enzyme bound	Mycobacterium tuberculosis
additional information	the substitution of iron with cobalt enhances the enzymatic activity of both wild-type and mutant PZase while zinc, magnesium and copper reduce it. Upon substitution of iron with zinc, magnesium and copper, PZase cannot function properly. Molecular level DFT based quantum mechanics computational analysis of mutant-metal substituted PZase complexes based on crystal structure PDB ID 3PL1, enzyme-metal binding analysis, overview	Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	I6XD65	-	-
Mycobacterium tuberculosis ATCC 25618	I6XD65	-	-
Mycobacterium tuberculosis H37Rv	I6XD65	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
PncA	-	Mycobacterium tuberculosis
PZAse	-	Mycobacterium tuberculosis

General Information

General Information	Comment	Organism
malfunction	cumulative effect of mutations and iron substitution	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)