1.5.3.1: sarcosine oxidase (formaldehyde-forming)
This is an abbreviated version!
For detailed information about sarcosine oxidase (formaldehyde-forming), go to the full flat file.
Word Map on EC 1.5.3.1
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1.5.3.1
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flavin
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fad
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heterotetrameric
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n-methylglycine
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creatininase
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amidinohydrolase
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n-methyltryptophan
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corynebacterial
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flavinylation
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diagnostics
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analysis
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medicine
- 1.5.3.1
- flavin
- fad
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heterotetrameric
- n-methylglycine
- creatininase
-
amidinohydrolase
- n-methyltryptophan
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corynebacterial
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flavinylation
- diagnostics
- analysis
- medicine
Reaction
Synonyms
heterotetrameric sarcosine oxidase, L-pipecolate oxidase, L-pipecolic acid oxidase, monomeric sarcosine oxidase, MSOX, PSO, sarcosine : oxygen oxidoreductase (demethylating), sarcosine oxidase, sarcosine: O2 oxidoreductase, sarcosine:oxygen oxidoreductase (demethylating), SO, SO-U96, SOX, SoxA, trd_1773, TSOX
ECTree
1.5.3.1 sarcosine oxidase (formaldehyde-forming)Advanced search results
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results (Engineering
Engineering on EC 1.5.3.1 - sarcosine oxidase (formaldehyde-forming)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C265A
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almost wild type activity but much more stable against thiol modifying inhibitors
C265D
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almost wild type activity but much more stable against thiol modifying inhibitors
C265R
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almost wild type activity but much more stable against thiol modifying inhibitors
C265S
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almost wild type activity but much more stable against thiol modifying inhibitors
C318S
C314A
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mutation of the covalent attachment site of FAD, mutant forms unstable complexes with FAD. In situ reconstitution of activity by assaying mutant in presence of FAD or 8-nor-8-chloro-FAD, giving a specific activity of 14% or 80% of wild-type, resp. Mutant exhibits high affinity for reduced flavin
C315A
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inactive, no bound FAD, forms stable non-covalent complex with 5-deazaFAD
H269N
His269 is probably not the active-site base but involved in interaction with substrate
H45A
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contains covalently bound FAD, 4fold less FAD than in wild type enzyme, catalytic properties similar than wild type enzyme, 50% of wild type activity
H45N
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contains covalently bound FAD, 4fold less FAD than in wild type enzyme, catalytic properties similar than wild type enzyme, 50% of wild type activity
K265A
K265M
K265Q
K265R
R49A
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inactive, no bound FAD, forms stable non-covalent complex with 5-deazaFAD
R49K
Y317F
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20fold decrease in the maxumim rate of the reductive half-reaction. Unlike wild-type, Kd-values of mutant are pH-dependent
K265A
Bacillus sp. (in: Bacteria) B-0618
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at least 250fold decrease in reaction rate. Crystallization analysis
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K265M
Bacillus sp. (in: Bacteria) B-0618
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at least 250fold decrease in reaction rate. Crystallization analysis
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K265Q
Bacillus sp. (in: Bacteria) B-0618
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at least 250fold decrease in reaction rate. Crystallization analysis
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K265R
Bacillus sp. (in: Bacteria) B-0618
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at least 250fold decrease in reaction rate. Crystallization analysis
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H173N
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leads to catalytically inactive beta subunit, study on organization of subunits and coenzymes
K171A
K171D
K171R
K358A
K358D
Y358R
the variant displays 0.07% activity and a higher apparent KM for sarcosine as compared to wild type enzyme
F235V/F339L
additional information
C318S
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modification of covalent flavin attachment site, mutant with extremely weak activity
K265A
at least 250fold decrease in reaction rate. Crystallization analysis
K265M
at least 250fold decrease in reaction rate. Crystallization analysis
K265Q
at least 250fold decrease in reaction rate. Crystallization analysis
K265R
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less than 30% of covalently bound FAD, strongly reduced turnover
K265R
at least 250fold decrease in reaction rate. Crystallization analysis
R49K
40fold decrease of turnover, 150fold decrease of catalytic efficiency, structure very similar to wild type enzyme
R49K
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contains covalently bound FAD, 4fold less FAD than in wild type enzyme, 4% of wild type activity
K171A
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39% activity of the wild-type enzyme, strongly increased Km for oxygen
K171A
the mutant shows 39% activity of the wild type enzyme
K171D
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32% activity of the wild-type enzyme, strongly increased Km for oxygen
K171D
the mutant shows 32% activity of the wild type enzyme
K171R
the mutant shows 58% activity of the wild type enzyme
additional information
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immobilization of the enzyme onto alkylamine and arylamine glass by crosslinking with glutaraldehyde for determination of serum sarcosine, method, overview. The enzyme shows a decrease in optimum pH and KM, and an increase in optimum temperature and time for linearity after immobilization
additional information
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production of soluble apoenzyme lacking covalently bound FAD by controlled expression in Escherichia coli. Reconstitution of enzyme by incubation with FAD
