Literature summary for 1.11.1.10 extracted from

Ghorbani Sangoli, M.; Housaindokht, M.R.; Bozorgmehr, M.R.
Effects of the deglycosylation on the structure and activity of chloroperoxidase molecular dynamics simulation approach (2020), J. Mol. Graph. Model., 97, 107570 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	in CPO, the sulfur atom in the Cys29 is located at the appropriate distance from the amide group of the Leu 32 and Glu 51 that leads to the hydrogen bonding formation of the amidesulfur groups, which is important for metalloproteins for the iron alignment	Leptoxyphium fumago

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
RH + chloride + H2O2	Leptoxyphium fumago	-	RCl + 2 H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Leptoxyphium fumago	P04963	Caldariomyces fumago	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	CPO enzyme contains thirteen sugars, including five N-acetyl D-glucosamines (NAG) and eight mannoses (MAN), which are attached to the protein via the glycosidic bonds. Analysis of the effects of the sugar segments on the structure and activity of CPO through the simulation of the halo structure and the structures without the sugar segment, overview. According to molecular dynamics simulation (MD), seven channels and fifteen cavities are identified in the CPO structure. Two of the channels provide the substrate access to the active site. The MD simulation results reveal that the removal of NAG decreases the number of the cavities from fifteen to eleven. Besides, the removal of NAG is associated with removing the channel providing the substrate access. The number of the cavities decreases from fifteen to fourteen through the removal of MAN, but, channel providing the substrate access to the active site is partly preserved. The MD simulation results indicate that the structures without the sugar units are more compact in comparison with the halo structures. The removal of the sugar segments induces the significant changes in the flexibility of the residues that affect the catalytic activity of the enzyme. As a result, the enzyme activities, such as the oxidation, alkylation, halogenation, and epoxidation cannot occur when the sugar segments of the enzyme are removed	Leptoxyphium fumago

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
RH + chloride + H2O2	-	Leptoxyphium fumago	RCl + 2 H2O	-	?

Synonyms

Synonyms	Comment	Organism
chloroperoxidase	-	Leptoxyphium fumago
CPO	-	Leptoxyphium fumago
heme-containing CPO	-	Leptoxyphium fumago

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
3	-	-	Leptoxyphium fumago

pH Range

pH Minimum	pH Maximum	Comment	Organism
3	6	high activity at	Leptoxyphium fumago

Cofactor

Cofactor	Comment	Organism	Structure
heme	the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited	Leptoxyphium fumago
additional information	the enzyme involves the protoporphyrin prosthetic group with the pI range of 3.2-4.0	Leptoxyphium fumago

pI Value

Organism	Comment	pI Value Maximum	pI Value
Leptoxyphium fumago	the enzyme involves the protoporphyrin prosthetic group with the pI range of 3.2-4.0	-	additional information

General Information

General Information	Comment	Organism
evolution	Caldariomyces fumago chloroperoxidase (CPO) is a glycosylated hemoprotein enzyme from the peroxidase family	Leptoxyphium fumago
malfunction	CPO enzyme contains thirteen sugars, including five N-acetyl D-glucosamines (NAG) and eight mannoses (MAN), which are attached to the protein via the glycosidic bonds. Removal of the sugars from CPO leads to increase the hydrophobicity of the enzyme, as well as the reduction of the alkylation reactions	Leptoxyphium fumago
additional information	computational molecular dynamics calculation, simulation, and modeling, using the glycosylated enzyme structure PDB ID 2CPO, overview	Leptoxyphium fumago
physiological function	the heme-containing CPO exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing the halogenation reactions. CPO selectively causes the oxidation and epoxidation of the diverse chemical compounds through the specific stereochemistry mechanism	Leptoxyphium fumago

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Release 2023.1 (January 2023)