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Information on EC 1.5.7.3 - N,N-dimethylglycine/sarcosine dehydrogenase (ferredoxin)
for references in articles please use BRENDA:EC1.5.7.3
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.7 With an iron-sulfur protein as acceptor
1.5.7.3 N,N-dimethylglycine/sarcosine dehydrogenase (ferredoxin)
IUBMB Comments
This bacterial enzyme is involved in degradation of glycine betaine. The enzyme contains non-covalently bound FAD and NAD(P) cofactors, and catalyses the demethylation of both N,N-dimethylglycine and sarcosine, releasing formaldehyde and forming glycine as the final product. The enzyme can utilize both NAD+ and NADP+, but the catalytic efficiency with NAD+ is ~5-fold higher. The native electron acceptor of the enzyme is a membrane-bound clostridial-type ferredoxin, which transfers the electrons to an electron-transfer flavoprotein (ETF).
The enzyme appears in viruses and cellular organisms
Reaction Schemes
show+
2
+
=
+
+
2
+
2
+
2
+
=
+
+
2
+
2
Synonyms
Csal0990, Csal_0990, DdhC, DgcA, DMG dehydrogenase, DMGDH, N,N-dimethylglycine/sarcosine dehydrogenase, PA5398, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Csal_0990
DdhC
DgcA
DMG dehydrogenase
DdhC
-
-
-
-
DgcA
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O = sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
(1)
-
-
-
sarcosine + 2 oxidized ferredoxin + H2O = glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
(2)
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
glycine betaine degradation III
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SYSTEMATIC NAME
IUBMB Comments
N,N-dimethylglycine/sarcosine:ferredoxin oxidoreductase (demethylating)
This bacterial enzyme is involved in degradation of glycine betaine. The enzyme contains non-covalently bound FAD and NAD(P) cofactors, and catalyses the demethylation of both N,N-dimethylglycine and sarcosine, releasing formaldehyde and forming glycine as the final product. The enzyme can utilize both NAD+ and NADP+, but the catalytic efficiency with NAD+ is ~5-fold higher. The native electron acceptor of the enzyme is a membrane-bound clostridial-type ferredoxin, which transfers the electrons to an electron-transfer flavoprotein (ETF).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis ATCC BAA-138
Substrates: -
Products: -
Products: -
?
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis CIP 106854
Substrates: -
Products: -
Products: -
?
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis NCIMB 13768
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis ATCC BAA-138
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis CIP 106854
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis NCIMB 13768
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: DdhC probably functions as an oxidoreductase, activity measurement using NAD+ or NADP+ with the PMS/DCPIP dye-linked system. Substrate specificity, overview. No show activity with trimethylamine, histamine, glycine betaine, or choline
Products: -
Products: -
-
additional information
?
-
Substrates: DdhC probably functions as an oxidoreductase, activity measurement using NAD+ or NADP+ with the PMS/DCPIP dye-linked system. Substrate specificity, overview. No show activity with trimethylamine, histamine, glycine betaine, or choline
Products: -
Products: -
-
additional information
?
-
Chromohalobacter israelensis ATCC BAA-138
Substrates: DdhC probably functions as an oxidoreductase, activity measurement using NAD+ or NADP+ with the PMS/DCPIP dye-linked system. Substrate specificity, overview. No show activity with trimethylamine, histamine, glycine betaine, or choline
Products: -
Products: -
-
additional information
?
-
Chromohalobacter israelensis CIP 106854
Substrates: DdhC probably functions as an oxidoreductase, activity measurement using NAD+ or NADP+ with the PMS/DCPIP dye-linked system. Substrate specificity, overview. No show activity with trimethylamine, histamine, glycine betaine, or choline
Products: -
Products: -
-
additional information
?
-
Substrates: DdhC probably functions as an oxidoreductase, activity measurement using NAD+ or NADP+ with the PMS/DCPIP dye-linked system. Substrate specificity, overview. No show activity with trimethylamine, histamine, glycine betaine, or choline
Products: -
Products: -
-
additional information
?
-
Chromohalobacter israelensis NCIMB 13768
Substrates: DdhC probably functions as an oxidoreductase, activity measurement using NAD+ or NADP+ with the PMS/DCPIP dye-linked system. Substrate specificity, overview. No show activity with trimethylamine, histamine, glycine betaine, or choline
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis ATCC BAA-138
Substrates: -
Products: -
Products: -
?
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis CIP 106854
Substrates: -
Products: -
Products: -
?
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
N,N-dimethylglycine + 2 oxidized ferredoxin + H2O
sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis NCIMB 13768
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis ATCC BAA-138
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis CIP 106854
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Substrates: -
Products: -
Products: -
?
sarcosine + 2 oxidized ferredoxin + H2O
glycine + formaldehyde + 2 reduced ferredoxin + 2 H+
Chromohalobacter israelensis NCIMB 13768
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
electron transferring flavoprotein
Etf, encoded by genes etfA (csal_0992) and etfB (csal_0993), SwissProt IDs Q1QYV9 and Q1QYV8
Ferredoxin
Csal0991 is a probable membrane-anchored ferredoxin (encoded by gene csal_0991, SwissProt ID Q1QYW0) that participates in the electron transfer process during N,N-dimethylglycine (DMG) degradation to sarcosine
-
additional information
enzyme DdhC does not need deliberate addition of metal ions to maintain its activity. No effects by added Na+, K+, Zn2+, Mn2+, Mg2+, Fe2+, and Co2+ at 2 mM. No activity is detected in the absence of NAD+ or NADP+ with the PMS/DCPIP dye-linked system, indicating that the enzyme is NAD(P)+-dependent
-
NAD+
prefers NAD+ to NADP+, Km and kcat values are 0.81 mM and 0.20 per sec, respectively
NAD+
Km is 0.81 mM, the enzyme exhibits dual coenzyme specificity, preferring NAD+ to NADP+
NADP+
prefers NAD+ to NADP+, Km and kcat values are 3.21 mM and 0.14 per sec, respectively
NADP+
Km is 3.21 mM, the enzyme exhibits dual coenzyme specificity, preferring NAD+ to NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
cofactor ferredoxin Csal0991 contains contains two [4Fe-4S] cluster-binding motifs (CX2CX2CX3CP, where X represents any amino acid residue), binding Fe2+
additional information
neither inhibitory nor activating: Na+, K+, Zn2+, Mn2+, Mg2+, Fe2+, Co2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
4 - 11
activity range, recombinant enzyme, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 80
activity range, recombinant enzyme, profile overview. DdhC shows 64% and 24% of maximal activity at 70°C and 80°C, respectively
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Chromohalobacter salexigens DSM 3043 can grow on N,N-dimethylglycine (DMG) as the sole C, N, and energy source and utilize sarcosine as the sole N source under aerobic conditions
brenda
-
Chromohalobacter salexigens DSM 3043 can grow on N,N-dimethylglycine (DMG) as the sole C, N, and energy source and utilize sarcosine as the sole N source under aerobic conditions
-
brenda
Chromohalobacter israelensis ATCC BAA-138
-
Chromohalobacter salexigens DSM 3043 can grow on N,N-dimethylglycine (DMG) as the sole C, N, and energy source and utilize sarcosine as the sole N source under aerobic conditions
-
brenda
Chromohalobacter israelensis CIP 106854
-
Chromohalobacter salexigens DSM 3043 can grow on N,N-dimethylglycine (DMG) as the sole C, N, and energy source and utilize sarcosine as the sole N source under aerobic conditions
-
brenda
-
Chromohalobacter salexigens DSM 3043 can grow on N,N-dimethylglycine (DMG) as the sole C, N, and energy source and utilize sarcosine as the sole N source under aerobic conditions
-
brenda
Chromohalobacter israelensis NCIMB 13768
-
Chromohalobacter salexigens DSM 3043 can grow on N,N-dimethylglycine (DMG) as the sole C, N, and energy source and utilize sarcosine as the sole N source under aerobic conditions
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
-
Proteins DgcA and DgcB are involved in conversion of dimethylglycine to sarcosine
physiological function
-
a mutant strain lacking DgcA accumulates dimethylglycine and glycine betaine when exposed to choline, resulting in hyperinduction of GbdR-regulated transcripts
physiological function
under high-salinity conditions, the presence of dimethylglycine inhibits growth of the wild type and induces the production and accumulation of trehalose and glucosylglycerate intracellularly. Exogenous addition of dimethylglycine significantly improves the growth rates of DdhC mutants incubated at 37°C synthetic medium with sarcosine as the sole N source
physiological function
the catabolism of N,N-dimethylglycine (DMG) results in release of ammonium
physiological function
-
under high-salinity conditions, the presence of dimethylglycine inhibits growth of the wild type and induces the production and accumulation of trehalose and glucosylglycerate intracellularly. Exogenous addition of dimethylglycine significantly improves the growth rates of DdhC mutants incubated at 37°C synthetic medium with sarcosine as the sole N source
-
physiological function
-
the catabolism of N,N-dimethylglycine (DMG) results in release of ammonium
-
physiological function
Chromohalobacter israelensis ATCC BAA-138
-
under high-salinity conditions, the presence of dimethylglycine inhibits growth of the wild type and induces the production and accumulation of trehalose and glucosylglycerate intracellularly. Exogenous addition of dimethylglycine significantly improves the growth rates of DdhC mutants incubated at 37°C synthetic medium with sarcosine as the sole N source
-
physiological function
Chromohalobacter israelensis ATCC BAA-138
-
the catabolism of N,N-dimethylglycine (DMG) results in release of ammonium
-
physiological function
Chromohalobacter israelensis CIP 106854
-
under high-salinity conditions, the presence of dimethylglycine inhibits growth of the wild type and induces the production and accumulation of trehalose and glucosylglycerate intracellularly. Exogenous addition of dimethylglycine significantly improves the growth rates of DdhC mutants incubated at 37°C synthetic medium with sarcosine as the sole N source
-
physiological function
Chromohalobacter israelensis CIP 106854
-
the catabolism of N,N-dimethylglycine (DMG) results in release of ammonium
-
physiological function
Chromohalobacter israelensis NCIMB 13768
-
under high-salinity conditions, the presence of dimethylglycine inhibits growth of the wild type and induces the production and accumulation of trehalose and glucosylglycerate intracellularly. Exogenous addition of dimethylglycine significantly improves the growth rates of DdhC mutants incubated at 37°C synthetic medium with sarcosine as the sole N source
-
physiological function
Chromohalobacter israelensis NCIMB 13768
-
the catabolism of N,N-dimethylglycine (DMG) results in release of ammonium
-
physiological function
-
under high-salinity conditions, the presence of dimethylglycine inhibits growth of the wild type and induces the production and accumulation of trehalose and glucosylglycerate intracellularly. Exogenous addition of dimethylglycine significantly improves the growth rates of DdhC mutants incubated at 37°C synthetic medium with sarcosine as the sole N source
-
physiological function
-
the catabolism of N,N-dimethylglycine (DMG) results in release of ammonium
-
additional information
a conserved dinucleotide-binding motif [GXGX2(G/A)X17(D/E), where X represents any amino acid residue] from residues 397 to 402, which is considered part of the Rossmann fold
additional information
-
a conserved dinucleotide-binding motif [GXGX2(G/A)X17(D/E), where X represents any amino acid residue] from residues 397 to 402, which is considered part of the Rossmann fold
-
additional information
Chromohalobacter israelensis ATCC BAA-138
-
a conserved dinucleotide-binding motif [GXGX2(G/A)X17(D/E), where X represents any amino acid residue] from residues 397 to 402, which is considered part of the Rossmann fold
-
additional information
Chromohalobacter israelensis CIP 106854
-
a conserved dinucleotide-binding motif [GXGX2(G/A)X17(D/E), where X represents any amino acid residue] from residues 397 to 402, which is considered part of the Rossmann fold
-
additional information
Chromohalobacter israelensis NCIMB 13768
-
a conserved dinucleotide-binding motif [GXGX2(G/A)X17(D/E), where X represents any amino acid residue] from residues 397 to 402, which is considered part of the Rossmann fold
-
additional information
-
a conserved dinucleotide-binding motif [GXGX2(G/A)X17(D/E), where X represents any amino acid residue] from residues 397 to 402, which is considered part of the Rossmann fold
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DDHC_CHRSD
Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)
694
0
76344
Swiss-Prot
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
monomer
1 * 77200, recombinant His6-tagged DdhC, SDS-PAGE, 1 * 78507, sequence calculation
monomer
-
1 * 77200, recombinant His6-tagged DdhC, SDS-PAGE, 1 * 78507, sequence calculation
-
monomer
Chromohalobacter israelensis ATCC BAA-138
-
1 * 77200, recombinant His6-tagged DdhC, SDS-PAGE, 1 * 78507, sequence calculation
-
monomer
Chromohalobacter israelensis CIP 106854
-
1 * 77200, recombinant His6-tagged DdhC, SDS-PAGE, 1 * 78507, sequence calculation
-
monomer
-
1 * 77200, recombinant His6-tagged DdhC, SDS-PAGE, 1 * 78507, sequence calculation
-
monomer
Chromohalobacter israelensis NCIMB 13768
-
1 * 77200, recombinant His6-tagged DdhC, SDS-PAGE, 1 * 78507, sequence calculation
-
additional information
the purified enzyme can exist in the form of a monomer, dimer, or polymer under nondenaturing conditions, but only the protein in the form of a monomer exhibits enzyme activity
additional information
-
the purified enzyme can exist in the form of a monomer, dimer, or polymer under nondenaturing conditions, but only the protein in the form of a monomer exhibits enzyme activity
-
additional information
Chromohalobacter israelensis ATCC BAA-138
-
the purified enzyme can exist in the form of a monomer, dimer, or polymer under nondenaturing conditions, but only the protein in the form of a monomer exhibits enzyme activity
-
additional information
Chromohalobacter israelensis CIP 106854
-
the purified enzyme can exist in the form of a monomer, dimer, or polymer under nondenaturing conditions, but only the protein in the form of a monomer exhibits enzyme activity
-
additional information
-
the purified enzyme can exist in the form of a monomer, dimer, or polymer under nondenaturing conditions, but only the protein in the form of a monomer exhibits enzyme activity
-
additional information
Chromohalobacter israelensis NCIMB 13768
-
the purified enzyme can exist in the form of a monomer, dimer, or polymer under nondenaturing conditions, but only the protein in the form of a monomer exhibits enzyme activity
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of mutant DELTAcsal_0990, two complemented strains CSDELTA0990(pBBR1MCS2-HBL90) and CSDELTA0990(pBBR1MCS2-HBS90) are able to grow in S-M63 with DMG as the sole N source, although their growth rates are significantly lower than that of the wild-type, while CSDELTA0990(pBBR1MCS2), as a negative control, is still unable to grow in the same medium. The four mutants (CSDELTA0990, CS?0991, CSDELTA0992, and CSDELTA0993) grow very slowly. Among them, CSDELTA0991 grows fastest
additional information
-
construction of mutant DELTAcsal_0990, two complemented strains CSDELTA0990(pBBR1MCS2-HBL90) and CSDELTA0990(pBBR1MCS2-HBS90) are able to grow in S-M63 with DMG as the sole N source, although their growth rates are significantly lower than that of the wild-type, while CSDELTA0990(pBBR1MCS2), as a negative control, is still unable to grow in the same medium. The four mutants (CSDELTA0990, CS?0991, CSDELTA0992, and CSDELTA0993) grow very slowly. Among them, CSDELTA0991 grows fastest
-
additional information
Chromohalobacter israelensis ATCC BAA-138
-
construction of mutant DELTAcsal_0990, two complemented strains CSDELTA0990(pBBR1MCS2-HBL90) and CSDELTA0990(pBBR1MCS2-HBS90) are able to grow in S-M63 with DMG as the sole N source, although their growth rates are significantly lower than that of the wild-type, while CSDELTA0990(pBBR1MCS2), as a negative control, is still unable to grow in the same medium. The four mutants (CSDELTA0990, CS?0991, CSDELTA0992, and CSDELTA0993) grow very slowly. Among them, CSDELTA0991 grows fastest
-
additional information
Chromohalobacter israelensis CIP 106854
-
construction of mutant DELTAcsal_0990, two complemented strains CSDELTA0990(pBBR1MCS2-HBL90) and CSDELTA0990(pBBR1MCS2-HBS90) are able to grow in S-M63 with DMG as the sole N source, although their growth rates are significantly lower than that of the wild-type, while CSDELTA0990(pBBR1MCS2), as a negative control, is still unable to grow in the same medium. The four mutants (CSDELTA0990, CS?0991, CSDELTA0992, and CSDELTA0993) grow very slowly. Among them, CSDELTA0991 grows fastest
-
additional information
-
construction of mutant DELTAcsal_0990, two complemented strains CSDELTA0990(pBBR1MCS2-HBL90) and CSDELTA0990(pBBR1MCS2-HBS90) are able to grow in S-M63 with DMG as the sole N source, although their growth rates are significantly lower than that of the wild-type, while CSDELTA0990(pBBR1MCS2), as a negative control, is still unable to grow in the same medium. The four mutants (CSDELTA0990, CS?0991, CSDELTA0992, and CSDELTA0993) grow very slowly. Among them, CSDELTA0991 grows fastest
-
additional information
Chromohalobacter israelensis NCIMB 13768
-
construction of mutant DELTAcsal_0990, two complemented strains CSDELTA0990(pBBR1MCS2-HBL90) and CSDELTA0990(pBBR1MCS2-HBS90) are able to grow in S-M63 with DMG as the sole N source, although their growth rates are significantly lower than that of the wild-type, while CSDELTA0990(pBBR1MCS2), as a negative control, is still unable to grow in the same medium. The four mutants (CSDELTA0990, CS?0991, CSDELTA0992, and CSDELTA0993) grow very slowly. Among them, CSDELTA0991 grows fastest
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
the purified recombinant enzyme is only stable at temperatures lower than 40°C and maintains 36% and less than 1% residual activities after incubation for 60 min at 50°C or 60°C, respectively
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified recombinant enzyme, 20 mM PBS buffer, pH 7.5, when stored at -20°C for 1 month in 50% glycerol, the enzyme activity remains almost unchanged
4°C, purified recombinant enzyme, 20 mM PBS buffer, pH 7.5, the activity decreases to 52% of its original level after incubation at 4°C for 72 h
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme DdhC from Escherichia coli by nickel affinity chromatography and gel filtration
recombinant protein, using Ni2x02-chelating affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene csal_0991, encoding enzyme DdhC, organized in an operon with csal_0992 and csal_0993, the operon comprises 5 or 6 genes, encoding the flavodoxin cofactor, recombinant overexpression of N-terminally His6-tagged enzyme DdhC in Escherichia coli strain BL21(DE3) as soluble protein. DdhC is also overexpressed as a C-terminally His6-tagged enzyme in Escherichi coli strain BL21(DE3), but the purified enzyme shows no activity, although the recombinant protein is soluble in Escherichia coli, indicating that addition of His-tag to the C-terminus of DdhC can seriously affect enzyme activity
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of genes GbcA, DgcA, and SoxA is induced in the presence of choline, glycine betaine, and dimethylglycine. Gene PA5380 is required for this induction
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fitzsimmons, L.; Flemer Jr., S.; Wurthmann, A.; Deker, P.; Sarkar, I.; Wargo, M.
Small-molecule inhibition of choline catabolism in Pseudomonas aeruginosa and other aerobic choline-catabolizing bacteria
Appl. Environ. Microbiol.
77
4383-4389
2011
Pseudomonas aeruginosa
brenda
Yang, T.; Shao, Y.H.; Guo, L.Z.; Meng, X.L.; Yu, H.; Lu, W.D.
Role of N,N-dimethylglycine and its catabolism to sarcosine in Chromohalobacter salexigens DSM 3043
Appl. Environ. Microbiol.
86
e01186
2020
Chromohalobacter israelensis (Q1QYW1), Chromohalobacter israelensis DSM 3043 (Q1QYW1), Chromohalobacter israelensis ATCC BAA-138 (Q1QYW1), Chromohalobacter israelensis CIP 106854 (Q1QYW1), Chromohalobacter israelensis NCIMB 13768 (Q1QYW1), Chromohalobacter israelensis 1H11 (Q1QYW1)
brenda
Wargo, M.; Szwergold, B.; Hogan, D.
Identification of two gene clusters and a transcriptional regulator required for Pseudomonas aeruginosa glycine betaine catabolism
J. Bacteriol.
190
2690-2699
2008
Pseudomonas aeruginosa
brenda
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