Literature summary for 1.5.3.1 extracted from

Xin, Y.; Zheng, M.; Wang, Q.; Lu, L.; Zhang, L.; Tong, Y.; Wang, W.
Structural and catalytic alteration of sarcosine oxidase through reconstruction with coenzyme-like ligands (2016), J. Mol. Catal. B, 133, S250-S258.

No PubMed abstract available

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21 (DE3) in the form of inclusion bodies. Unfolded Bacillus sp. SOX was extracted from an inclusion body and reconstructed with FAD and a group of coenzyme-like compounds. The interactions between the enzyme and various ligands are simulated using molecular docking in the SwissDock service and DS 2.5 program. When the length of the ligand is reduced, the number of H bonds is also reduced. Furthermore, new bonds are formed between the enzyme and the ligands, owing to replacements at the position 7- or 8-sites. Based on the results of structural analysis, phosphoric acid and adenine groups in the natural coenzyme likely play vital roles in maintenance of the enzyme structure. The 7-and 8-site modifications in ligands could facilitate the formation of novel interactions that stabilize the complex. The activities of natural enzyme and refolded FAD-enzyme aree significantly reduced in the presence of organic solvents. However, when the enzyme is refolded with coenzyme-like ligands containing halogen atoms at the position 7- or 8-site, the trend towards reduction is effectively inhibited, and the enzymes exhibit considerably higher relative specificities	Bacillus sp. (in: Bacteria)

Cloned (Comment)

Organism

expressed in Escherichia coli BL21 (DE3) in the form of inclusion bodies. Unfolded Bacillus sp. SOX was extracted from an inclusion body and reconstructed with FAD and a group of coenzyme-like compounds. The interactions between the enzyme and various ligands are simulated using molecular docking in the SwissDock service and DS 2.5 program. When the length of the ligand is reduced, the number of H bonds is also reduced. Furthermore, new bonds are formed between the enzyme and the ligands, owing to replacements at the position 7- or 8-sites. Based on the results of structural analysis, phosphoric acid and adenine groups in the natural coenzyme likely play vital roles in maintenance of the enzyme structure. The 7-and 8-site modifications in ligands could facilitate the formation of novel interactions that stabilize the complex. The activities of natural enzyme and refolded FAD-enzyme aree significantly reduced in the presence of organic solvents. However, when the enzyme is refolded with coenzyme-like ligands containing halogen atoms at the position 7- or 8-site, the trend towards reduction is effectively inhibited, and the enzymes exhibit considerably higher relative specificities

Bacillus sp. (in: Bacteria)

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
141.6	-	sarcosine	native enzyme, reconstructed in aqueous, pH 8.0, 37°C	Bacillus sp. (in: Bacteria)
142.3	-	sarcosine	native enzyme, reconstructed with 20% dimethyl sulfoxide, pH 8.0, 37°C	Bacillus sp. (in: Bacteria)

Organism

Organism	UniProt	Comment	Textmining
Bacillus sp. (in: Bacteria)	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
sarcosine + H2O + O2	-	Bacillus sp. (in: Bacteria)	glycine + formaldehyde + H2O2	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Bacillus sp. (in: Bacteria)

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.115	-	sarcosine	native enzyme, reconstructed with 20% dimethyl sulfoxide, pH 8.0, 37°C	Bacillus sp. (in: Bacteria)
0.204	-	sarcosine	native enzyme, reconstructed in aqueous, pH 8.0, 37°C	Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Bacillus sp. (in: Bacteria)

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.000808	-	sarcosine	native enzyme, reconstructed with 20% dimethyl sulfoxide, pH 8.0, 37°C	Bacillus sp. (in: Bacteria)
0.00144	-	sarcosine	native enzyme, reconstructed in aqueous, pH 8.0, 37°C	Bacillus sp. (in: Bacteria)