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Literature summary for 1.13.11.20 extracted from

  • Dominy, J.E.; Simmons, C.R.; Karplus, P.A.; Gehring, A.M.; Stipanuk, M.H.
    Identification and characterization of bacterial cysteine dioxygenases: a new route of cysteine degradation for eubacteria (2006), J. Bacteriol., 188, 5561-5569.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Rattus norvegicus
the open reading frame of putative cysteine dioxygenase NP_390992(yubC, Bacillus subtilis) is cloned and overexpressed in Escherichia coli. Bacillus subtilis
the open reading frame of putative cysteine dioxygenase NP_627257 (SCO30335, Streptomyces coelicolor A3(2))is cloned and overexpressed in Escherichia coli Streptomyces coelicolor
the open reading frame of putative cysteine dioxygenase NP_629897 (SCO5772, Streptomyces coelicolor A3(2)) is cloned and overexpressed in Escherichia coli Streptomyces coelicolor
the open reading frame of putative cysteine dioxygenase NP_832375(BC2617, Bacillus cereus ATCC 14579) is cloned and overexpressed in Escherichia coli Bacillus cereus

Inhibitors

Inhibitors Comment Organism Structure
2-amino-ethanethiol 1 x the Km for cysteine = -2.5% inhibition, 10 x the Km for cysteine = 20% inhibition Bacillus cereus
2-amino-ethanethiol YubC: 1 x the Km for cysteine = 12% inhibition, 10 x the Km for cysteine = 19% inhibition Bacillus subtilis
2-amino-ethanethiol 1 x the Km for cysteine = 8.7% inhibition, 10 x the Km for cysteine = 30% inhibition Rattus norvegicus
2-amino-ethanethiol SCO3035: 1 x the Km for cysteine = 7.5% inhibition, 10 x the Km for cysteine = 27% inhibition; SCO5772: 1 x the Km for cysteine = 0.9% inhibition, 10 x the Km for cysteine = 28% inhibition Streptomyces coelicolor
2-sulfanyl-ethanol 1 x the Km for cysteine = 4.8% inhibition, 10 x the Km for cysteine = 11% inhibition Bacillus cereus
2-sulfanyl-ethanol YubC: 1 x the Km for cysteine = -0.7% inhibition, 10 x the Km for cysteine = 6.6% inhibition Bacillus subtilis
2-sulfanyl-ethanol 1 x the Km for cysteine = 5.9% inhibition, 10 x the Km for cysteine = 13% inhibition Rattus norvegicus
2-sulfanyl-ethanol SCO3035: 1 x the Km for cysteine = 8.6% inhibition, 10 x the Km for cysteine = 15% inhibition; SCO5772: 1 x the Km for cysteine = 2.6% inhibition, 10 x the Km for cysteine = 13% inhibition Streptomyces coelicolor
3-sulfanyl-propionic acid 1 x the Km for cysteine = 3.2% inhibition, 10 x the Km for cysteine = 12% inhibition Bacillus cereus
3-sulfanyl-propionic acid YubC: 1 x the Km for cysteine = 4.7% inhibition, 10 x the Km for cysteine = 11% inhibition Bacillus subtilis
3-sulfanyl-propionic acid 1 x the Km for cysteine = 4.9% inhibition, 10 x the Km for cysteine = 26% inhibition Rattus norvegicus
3-sulfanyl-propionic acid SCO3035: 1 x the Km for cysteine = 2.9% inhibition, 10 x the Km for cysteine = 11% inhibition; SCO5772: 1 x the Km for cysteine = 5.6% inhibition, 10 x the Km for cysteine = 16% inhibition Streptomyces coelicolor

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2
-
L-cysteine SCO3035, measurement of cysteine sulfinic acid production is done by high-performance liquid chromatography Streptomyces coelicolor
1.5
-
L-cysteine measurement of cysteine sulfinic acid production is done by high-performance liquid chromatography Rattus norvegicus
3
-
cysteine YubC, measurement of cysteine sulfinic acid production is done by high-performance liquid chromatography Bacillus subtilis
3.8
-
L-cysteine SCO5772, measurement of cysteine sulfinic acid production is done by high-performance liquid chromatography Streptomyces coelicolor
5.7
-
L-cysteine measurement of cysteine sulfinic acid production is done by high-performance liquid chromatography Bacillus cereus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ upon purification the protein is catalytically inactive, activity can be restored upon the addition of exogenous ferrous iron, with maximal activation at a ferrous iron concentration of 0.3 mM Streptomyces coelicolor
Fe2+ upon purification the protein is catalytically inactive, activity can be restored upon the addition of exogenous ferrous iron, with maximal activation at a ferrous iron concentration of 0.3 mM Bacillus cereus
Fe2+ YubC: Upon purification the protein is catalytically inactive, activity can be restored upon the addition of exogenous ferrous iron, with maximal activation at a ferrous iron concentration of 0.3 mM Bacillus subtilis
additional information Co2+ fails to restore significant activity to purified proteins Streptomyces coelicolor
additional information Co2+ fails to restore significant activity to purified proteins Bacillus cereus
additional information Mn2+ fails to restore significant activity to purified proteins Streptomyces coelicolor
additional information Mn2+ fails to restore significant activity to purified proteins Bacillus cereus
additional information Ni2+ fails to restore significant activity to purified proteins Streptomyces coelicolor
additional information Ni2+ fails to restore significant activity to purified proteins Bacillus cereus
additional information YubC: Co2+ fails to restore significant activity to purified proteins Bacillus subtilis
additional information YubC: Mn2+ fails to restore significant activity to purified proteins Bacillus subtilis
additional information YubC: Ni2+ fails to restore significant activity to purified proteins Bacillus subtilis
additional information YubC: Zn2+ fails to restore significant activity to purified proteins Bacillus subtilis
additional information Zn2+ fails to restore significant activity to purified proteins Streptomyces coelicolor
additional information Zn2+ fails to restore significant activity to purified proteins Bacillus cereus

Organism

Organism UniProt Comment Textmining
Bacillus cereus Q81CX4 BC2617 has 13.0% sequence identity with rat CDO, calculated by a BLASTP alignment using VEctor NTI; BC2617
-
Bacillus cereus DSM 31 Q81CX4 BC2617 has 13.0% sequence identity with rat CDO, calculated by a BLASTP alignment using VEctor NTI; BC2617
-
Bacillus subtilis O32085 YubC has 18.7% sequence identity with rat CDO, calculated by a BLASTP alignment using Vector NTI; wild-type strain 168 and strain 168 YubC::pMUTIN4 and yubC, CDO activity is detectable in wild-type Bacillus subtilis during vegetative growth and increses to ~350% 10 h after sporulation induction. Neither yubC gene expression nor CDO catalytic activity can be detected in the yubC::pMUTIN4 strain.
-
no activity in Nostoc sp.
-
strain PCC73102
-
Rattus norvegicus P21816
-
-
Streptomyces coelicolor O50490 SCO5772 has 16.4% sequence identity with rat CDO, calculated by a BLASTP alignment using Vector NTI; A3(2) SCO5772
-
Streptomyces coelicolor Q9KZL0 SCO3035 has 20.6% sequence identity with rat CDO, calculated by a BLASTP alignment using VEctor NTI; A3(2) SCO3035
-
Streptomyces coelicolor A3(2) SCO3035 Q9KZL0 SCO3035 has 20.6% sequence identity with rat CDO, calculated by a BLASTP alignment using VEctor NTI; A3(2) SCO3035
-
Streptomyces coelicolor A3(2) SCO5772 O50490 SCO5772 has 16.4% sequence identity with rat CDO, calculated by a BLASTP alignment using Vector NTI; A3(2) SCO5772
-

Purification (Commentary)

Purification (Comment) Organism
-
Rattus norvegicus
HisTrap HP column, immobilized metal affinity chromatography Streptomyces coelicolor
HisTrap HP column, immobilized metal affinity chromatography, during purification of SCO30335 two peaks of highly purified recombinant protein are found to elute: one at 10% (peak1) and the second at 20% (peak 2), kinetic data show that peak 1 has lower Km and higher Vmax values for cysteine than peak 2 Streptomyces coelicolor
HisTrap HP column, immobilized metal affinity chromatography, during purification two peaks of highly purified recombinant protein are found to elute: one at 10% (peak1) and the second at 20% (peak 2), kinetic data show that peak 1 has lower Km and higher Vmax values for cysteine than peak 2 Bacillus cereus
HisTrap HP column, immobilized metal affinity chromatography, during purification two peaks of highly purified recombinant protein are found to elute: one at 10% (peak1) and the second at 20%(peak 2), kinetic datat show that peak 1 has lower Km and higher Vmax values for cysteine thant peak 2. Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.7
-
SCO5772 Streptomyces coelicolor
0.8
-
SCO3035 Streptomyces coelicolor
1
-
YubC Bacillus subtilis
1.4
-
-
Rattus norvegicus
4.4
-
-
Bacillus cereus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + O2
-
Streptomyces coelicolor 3-sulfino-L-alanine
-
?
L-cysteine + O2
-
Bacillus subtilis 3-sulfino-L-alanine
-
?
L-cysteine + O2
-
Bacillus cereus 3-sulfino-L-alanine
-
?
L-cysteine + O2
-
Rattus norvegicus 3-sulfino-L-alanine
-
?
L-cysteine + O2
-
Streptomyces coelicolor A3(2) SCO3035 3-sulfino-L-alanine
-
?
L-cysteine + O2
-
Bacillus cereus DSM 31 3-sulfino-L-alanine
-
?
L-cysteine + O2
-
Streptomyces coelicolor A3(2) SCO5772 3-sulfino-L-alanine
-
?

Synonyms

Synonyms Comment Organism
CDO
-
no activity in Nostoc sp.
CDO
-
Streptomyces coelicolor
CDO
-
Bacillus subtilis
CDO
-
Bacillus cereus
CDO
-
Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.3
-
L-cysteine SCO5772 Streptomyces coelicolor
0.33
-
L-cysteine SCO3035 Streptomyces coelicolor
0.39
-
L-cysteine YubC Bacillus subtilis
0.62
-
L-cysteine
-
Rattus norvegicus
2
-
L-cysteine
-
Bacillus cereus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
SCO3035, pH optimum is determined by using 2-morpholinoethanesulfonic acid or Tris buffers at a final concentration of 62.5 mM Streptomyces coelicolor
6.1
-
pH optimum is determined by using 2-morpholinoethanesulfonic acid or Tris buffers at a final concentration of 62.5 mM Bacillus cereus
6.1
-
pH optimum is determined by using 2-morpholinoethanesulfonic acid or Tris buffers at a final concentration of 62.5 mM Rattus norvegicus
6.1
-
SCO5772, pH optimum is determined by using 2-morpholinoethanesulfonic acid or Tris buffers at a final concentration of 62.5 mM Streptomyces coelicolor
6.2
-
YubC, pH optimum is determined by using 2-morpholinoethanesulfonic acid or Tris buffers at a final concentration of 62.5 mM Bacillus subtilis