Sarcosine oxidase
Sarcosine oxidase structure
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Common Name | Sarcosine oxidase | ||
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| CAS Number | 9029-22-5 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Initial characterization of the human central proteome.
BMC Syst. Biol. 5 , 17, (2011) On the basis of large proteomics datasets measured from seven human cell lines we consider their intersection as an approximation of the human central proteome, which is the set of proteins ubiquitously expressed in all human cells. Composition and properties... |
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Complete sequencing and characterization of 21,243 full-length human cDNAs.
Nat. Genet. 36 , 40-5, (2004) As a base for human transcriptome and functional genomics, we created the "full-length long Japan" (FLJ) collection of sequenced human cDNAs. We determined the entire sequence of 21,243 selected clones and found that 14,490 cDNAs (10,897 clusters) were unique... |
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res. 14 , 2121-7, (2004) The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a r... |
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Covalent flavinylation of monomeric sarcosine oxidase: identification of a residue essential for holoenzyme biosynthesis.
Biochemistry 47(4) , 1136-43, (2008) FAD in monomeric sarcosine oxidase (MSOX) is covalently linked to the protein by a thioether linkage between its 8alpha-methyl group and Cys315. Covalent flavinylation of apoMSOX has been shown to proceed via an autocatalytic reaction that requires only FAD a... |
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Analytical expression of non-steady-state concentrations and current pertaining to compounds present in the enzyme membrane of biosensor.
J. Phys. Chem. A 115(17) , 4299-306, (2011) A mathematical model of trienzyme biosensor at an internal diffusion limitation for a non-steady-state condition has been developed. The model is based on diffusion equations containing a linear term related to Michaelis-Menten kinetics of the enzymatic react... |
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Kinetic studies on the role of Lys-171 and Lys-358 in the beta subunit of sarcosine oxidase from Corynebacterium sp. U-96.
J. Biochem. 141(6) , 799-815, (2007) Heterotetrameric sarcosine oxidase from Corynebacterium sp.U-96(SO-U96) contains non-covalent and covalent flavins. Lys-358 and Lys-171 in the beta subunit is present at non-covalent flavin adenine dinucleotide (FAD)- and covalent flavin monodinucleotide (FMN... |
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Deuterium kinetic isotope effects in heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96: the anionic form of the substrate in the enzyme-substrate complex is a reactive species.
J. Biochem. 151(6) , 633-42, (2012) Heterotetrameric sarcosine oxidase is a flavoprotein that catalyses the oxidative demethylation of sarcosine. It is thought that the dehydrogenated substrate is the anionic form of sarcosine. To verify this assumption, the rate of flavin-adenine dinucleotide ... |
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Sarcosine metabolism in Haemonchus contortus and Teladorsagia circumcincta.
Exp. Parasitol. 134(1) , 1-6, (2013) Sarcosine (N-methylglycine) is an intermediate in glycine degradation and can also be synthesised from glycine in mammals. Sarcosine metabolism in Haemonchus contortus and Teladorsagia circumcincta differed from that of mammals in that creatinase activity was... |
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Probing oxygen activation sites in two flavoprotein oxidases using chloride as an oxygen surrogate.
Biochemistry 50(24) , 5521-34, (2011) A single basic residue above the si-face of the flavin ring is the site of oxygen activation in glucose oxidase (GOX) (His516) and monomeric sarcosine oxidase (MSOX) (Lys265). Crystal structures of both flavoenzymes exhibit a small pocket at the oxygen activa... |
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Structural characterization of mutations at the oxygen activation site in monomeric sarcosine oxidase .
Biochemistry 49(17) , 3631-9, (2010) Oxygen reduction and sarcosine oxidation in monomeric sarcosine oxidase (MSOX) occur at separate sites above the si- and re-faces, respectively, of the flavin ring. Mutagenesis studies implicate Lys265 as the oxygen activation site. Substitution of Lys265 wit... |