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ATP + sirohydrochlorin + Co2+
ADP + phosphate + Co(II)-sirohydrochlorin + H+
ATP + sirohydrochlorin + Fe2+
ADP + phosphate + Fe(II)-sirohydrochlorin + H+
cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+
precorrin-2 + Co2+
Co-precorrin-2 + H+
precorrin-2 + Co2+
cobalt-precorrin-2 + H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
sirohydrochlorin + Fe2+
iron-sirohydrochlorin + 2 H+
sirohydrochlorin + Fe2+
siroheme + H+
additional information
?
-
ATP + sirohydrochlorin + Co2+
ADP + phosphate + Co(II)-sirohydrochlorin + H+
-
-
-
?
ATP + sirohydrochlorin + Co2+
ADP + phosphate + Co(II)-sirohydrochlorin + H+
-
-
-
?
ATP + sirohydrochlorin + Fe2+
ADP + phosphate + Fe(II)-sirohydrochlorin + H+
-
-
-
?
ATP + sirohydrochlorin + Fe2+
ADP + phosphate + Fe(II)-sirohydrochlorin + H+
-
-
-
?
cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+
-
-
-
-
?
cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+
-
-
-
-
?
precorrin-2 + Co2+
Co-precorrin-2 + H+
-
-
-
?
precorrin-2 + Co2+
Co-precorrin-2 + H+
-
-
-
?
precorrin-2 + Co2+
Co-precorrin-2 + H+
-
tetrapyrrole biosynthesis, formation of tetrapyrrole cofactors
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
-
involved in the formation of a octahedrally co-ordinated cobalt ion. In the oxygen-dependent cobalamin, i.e. vitamin B12, biosynthetic pathway, cobalt is inserted into a ring-contracted tetrapyrrole called hydrogenobyrinic acid a,c-diamide, HBAD, by a cobaltochelatase that is constituted by three subunits, CobN, CobS and CobT
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
a step involved in the vitamin B12 biosynthesis
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
both CbiKP and DELTA28CbiKP insert cobalt and iron into sirohydrochlorin with specific activity with iron lower than that measured with cobalt
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
the enzyme inserts cobalt and iron into sirohydrochlorin with specific activity with iron lower than that measured with cobalt
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
a step involved in the vitamin B12 biosynthesis
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
the enzyme inserts cobalt and iron into sirohydrochlorin with specific activity with iron lower than that measured with cobalt
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
both CbiKP and DELTA28CbiKP insert cobalt and iron into sirohydrochlorin with specific activity with iron lower than that measured with cobalt
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
Methanobacter thermoautotrophicum
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
Methanobacter thermoautotrophicum
-
cobalamin biosynthetic pathway
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
cobalamin biosynthetic pathway
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
cobalamin biosynthetic pathway
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
biosynthesis of vitamin B12
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
biosynthesis of vitamin B12
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
cobalamin and siroheme biosynthesis,cbiK is able to substitute for cysG
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
cobalamin branched biosynthetic pathway
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
biosynthesis of vitamin B12
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis, oxygen-independent pathway
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis, oxygen-independent pathway
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
-
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis, oxygen-independent route, CbiK is a biglobal enzyme containing 2 a/b domains, which generate an active site with a deep rectangular cleft at their interface
-
?
sirohydrochlorin + Fe2+
iron-sirohydrochlorin + 2 H+
-
-
-
?
sirohydrochlorin + Fe2+
iron-sirohydrochlorin + 2 H+
both CbiKP and DELTA28CbiKP insert cobalt and iron into sirohydrochlorin with specific activity with iron lower than that measured with cobalt
-
-
?
sirohydrochlorin + Fe2+
iron-sirohydrochlorin + 2 H+
the enzyme inserts cobalt and iron into sirohydrochlorin with specific activity with iron lower than that measured with cobalt
-
-
?
sirohydrochlorin + Fe2+
siroheme + H+
Methanobacter thermoautotrophicum
-
CbiXS can act as a ferrochelatase in the biosynthesis of siroheme in vivo
-
?
sirohydrochlorin + Fe2+
siroheme + H+
-
CbiXS can act as a ferrochelatase in the biosynthesis of siroheme in vivo
-
?
sirohydrochlorin + Fe2+
siroheme + H+
-
CbiXS can act as a ferrochelatase in the biosynthesis of siroheme in vivo
-
?
additional information
?
-
-
CbiK fused together with CbiL as a multifunctional protein
-
?
additional information
?
-
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
?
additional information
?
-
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
?
additional information
?
-
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
?
additional information
?
-
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
?
additional information
?
-
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
?
additional information
?
-
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
?
additional information
?
-
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
?
additional information
?
-
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
?
additional information
?
-
Methanobacter thermoautotrophicum
-
precorrin-2 is no substrate
-
?
additional information
?
-
-
precorrin-2 is no substrate
-
?
additional information
?
-
-
precorrin-2 is no substrate
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+
precorrin-2 + Co2+
Co-precorrin-2 + H+
-
tetrapyrrole biosynthesis, formation of tetrapyrrole cofactors
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
sirohydrochlorin + Fe2+
iron-sirohydrochlorin + 2 H+
-
-
-
?
sirohydrochlorin + Fe2+
siroheme + H+
additional information
?
-
cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+
-
-
-
-
?
cobalt-sirohydrochlorin + H+
sirohydrochlorin + Co2+
-
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
-
involved in the formation of a octahedrally co-ordinated cobalt ion. In the oxygen-dependent cobalamin, i.e. vitamin B12, biosynthetic pathway, cobalt is inserted into a ring-contracted tetrapyrrole called hydrogenobyrinic acid a,c-diamide, HBAD, by a cobaltochelatase that is constituted by three subunits, CobN, CobS and CobT
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
a step involved in the vitamin B12 biosynthesis
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
a step involved in the vitamin B12 biosynthesis
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
Methanobacter thermoautotrophicum
-
cobalamin biosynthetic pathway
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
cobalamin biosynthetic pathway
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
cobalamin biosynthetic pathway
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
biosynthesis of vitamin B12
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
biosynthesis of vitamin B12
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
cobalamin and siroheme biosynthesis,cbiK is able to substitute for cysG
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
cobalamin branched biosynthetic pathway
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
biosynthesis of vitamin B12
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis, oxygen-independent pathway
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis, oxygen-independent pathway
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis, oxygen-independent route, CbiK is a biglobal enzyme containing 2 a/b domains, which generate an active site with a deep rectangular cleft at their interface
-
?
sirohydrochlorin + Fe2+
siroheme + H+
Methanobacter thermoautotrophicum
-
CbiXS can act as a ferrochelatase in the biosynthesis of siroheme in vivo
-
?
sirohydrochlorin + Fe2+
siroheme + H+
-
CbiXS can act as a ferrochelatase in the biosynthesis of siroheme in vivo
-
?
sirohydrochlorin + Fe2+
siroheme + H+
-
CbiXS can act as a ferrochelatase in the biosynthesis of siroheme in vivo
-
?
additional information
?
-
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
?
additional information
?
-
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
?
additional information
?
-
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
?
additional information
?
-
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
?
additional information
?
-
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
?
additional information
?
-
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
?
additional information
?
-
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
?
additional information
?
-
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
?
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137000
-
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
14300
SDS-PAGE, His-tagged protein of mutant M76
14900
SDS-PAGE, His-tagged wild type protein
17000
Methanobacter thermoautotrophicum
-
SDS-PAGE
17200
SDS-PAGE, His-tagged protein of mutant M200
17500
SDS-PAGE, His-tagged protein of mutant M54
17800
SDS-PAGE, His-tagged protein of mutant M136
18400
SDS-PAGE, His-tagged protein of mutant M150
18600
SDS-PAGE, His-tagged protein of mutant M10
18700
SDS-PAGE, His-tagged protein of mutant M508
20100
SDS-PAGE, His-tagged protein of mutant M507
23000
-
x * 23000, SDS-PAGE
25300
SDS-PAGE, His-tagged protein of mutant M518
27000
SDS-PAGE, His-tagged protein of mutant M51
28000
x * 28000, SDS-PAGE and calculated, mature protein
37000
-
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
71000
-
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
14000
-
gene-predicted molecular mass
14000
Methanobacter thermoautotrophicum
-
gene-predicted molecular mass
31000
x * 31000, recombinant enzyme, SDS-PAGE
31000
x * 31000, PAGE and calculated, mature protein
40000
-
gel filtration
40000
Methanobacter thermoautotrophicum
-
gel filtration
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E184L
mutation in metal binding site, about 3fold increase in activity
E184L/H216L
mutation in metal binding site, strong decrease in activity
H154L
mutation in metal binding site. Mutant has negligible activity
H154L/E184L
mutation in metal binding site, negligible activity
H154L/E184L/H216L
mutation in metal binding site. Mutant has negligible activity
H154L/H216L
mutation in metal binding site. Mutant has negligible activity
H216L
mutation in metal binding site. Mutant has negligible activity
E184L
-
mutation in metal binding site, about 3fold increase in activity
-
H154L
-
mutation in metal binding site. Mutant has negligible activity
-
H154L/E184L
-
mutation in metal binding site, negligible activity
-
H154L/H216L
-
mutation in metal binding site. Mutant has negligible activity
-
H216L
-
mutation in metal binding site. Mutant has negligible activity
-
C259S
-
site-directed mutagenesis
C262S
-
site-directed mutagenesis
M257L
-
site-directed mutagenesis
C259S
-
site-directed mutagenesis
-
C262S
-
site-directed mutagenesis
-
M257L
-
site-directed mutagenesis
-
H145A/H207A
-
site-directed mutagenesis
H192A
double mutation in M51 mutant
H192A
double mutation in M518 mutant
H78A
double mutation in M51 mutant
additional information
CbiKc gene is able to complement an Escherichia coli cysG mutant
additional information
CbiKc gene is able to complement an Escherichia coli cysG mutant
additional information
CbiKp gene is able to complement an Escherichia coli cysG mutant
additional information
CbiKp gene is able to complement an Escherichia coli cysG mutant
additional information
construction of a truncated DVU0650 protein that starts at amino acid 29, resulting in mutant DELTA28DVU0650. A truncated protein that lacks the signal peptide is also produced, named DELTA28CbiKP
additional information
construction of a truncated DVU0650 protein that starts at amino acid 29, resulting in mutant DELTA28DVU0650. A truncated protein that lacks the signal peptide is also produced, named DELTA28CbiKP
additional information
-
CbiKc gene is able to complement an Escherichia coli cysG mutant
-
additional information
-
CbiKp gene is able to complement an Escherichia coli cysG mutant
-
additional information
-
construction of a truncated DVU0650 protein that starts at amino acid 29, resulting in mutant DELTA28DVU0650. A truncated protein that lacks the signal peptide is also produced, named DELTA28CbiKP
-
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Schubert, H.L.; Raux, E.; Wilson, K.S.; Warren, M.J.
Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis
Biochemistry
38
10660-10669
1999
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Brindley, A.A.; Raux E.; Leech, H.K.; Schubert, H.L.; Warren, M.J.
A story of chelatase evolution: Identification and characterisation of a small 13-15 kDa 'ancestral' cobaltochelatase (CbiXS) in the Archaea
J. Biol. Chem.
278
22388-22395
2003
Methanosarcina barkeri, Methanobacter thermoautotrophicum, Methanosarcina barkeri Fusaro / DSM 804
brenda
Schubert, H.L.; Raux, E.; Matthews, M.A.; Phillips, J.D.; Wilson, K.S.; Hill, C.P.; Warren, M.J.
Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase
Biochem. Soc. Trans.
30
595-600
2002
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Leech, H.K.; Raux-Deery, E.; Heathcote, P.; Warren, M.J.
Production of cobalamin and sirohaem in Bacillus megaterium: an investigation into the role of the branchpoint chelatases sirohydrochlorin ferrochelatase (SirB) and sirohydrochlorin cobalt chelatase (CbiX)
Biochem. Soc. Trans.
30
610-613
2002
Priestia megaterium
brenda
Raux, E.; Schubert, H.L.; Warren, M.J.
Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum
Cell. Mol. Life Sci.
57
1880-1893
2000
Priestia megaterium, Porphyromonas gingivalis, Clostridium acetobutylicum, Clostridioides difficile, no activity in Bacillus subtilis, Pseudomonas aeruginosa, Cereibacter sphaeroides, Salmonella enterica subsp. enterica serovar Typhimurium, no activity in eukaryota
brenda
Raux, E.; Thermes, C.; Heathcote, P.; Rambach, A.; Warren, M.J.
A role for Salmonella typhimurium cbiK in cobalamin (vitamin B12) and siroheme biosynthesis
J. Bacteriol.
179
3202-3212
1997
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Leech, H.K.; Raux, E.; McLean, K.J.; Munro, A.W.; Robinson, N.J.; Borrelly, G.P.; Malten, M.; Jahn, D.; Rigby, S.E.; Heathcote, P.; Warren, M.J.
Characterization of the cobaltochelatase CbiXL: evidence for a 4Fe-4S center housed within an MXCXXC motif
J. Biol. Chem.
278
41900-41907
2003
Synechocystis sp., Priestia megaterium, Priestia megaterium DSM 509
brenda
Yin, J.; Xu, L.X.; Cherney, M.M.; Raux-Deery, E.; Bindley, A.A.; Savchenko, A.; Walker, J.R.; Cuff, M.E.; Warren, M.J.; James, M.N.
Crystal structure of the vitamin B12 biosynthetic cobaltochelatase, CbiXS, from Archaeoglobus fulgidus
J. Struct. Funct. Genomics
7
37-50
2006
Archaeoglobus fulgidus (O29537)
brenda
Pisarchik, A.; Petri, R.; Schmidt-Dannert, C.
Probing the structural plasticity of an archaeal primordial cobaltochelatase CbiXS
Protein Eng. Des. Sel.
20
257-265
2007
Methanosarcina barkeri (P61816)
brenda
Lobo, S.A.; Brindley, A.A.; Romao, C.V.; Leech, H.K.; Warren, M.J.; Saraiva, L.M.
Two distinct roles for two functional cobaltochelatases (CbiK) in Desulfovibrio vulgaris Hildenborough
Biochemistry
47
5851-5857
2008
Desulfovibrio vulgaris (Q72CB8), Desulfovibrio vulgaris (Q72EC8), Desulfovibrio vulgaris Hildenborough (Q72CB8), Desulfovibrio vulgaris Hildenborough (Q72EC8)
brenda
Lundqvist, J.; Elmlund, D.; Heldt, D.; Deery, E.; Soederberg, C.A.; Hansson, M.; Warren, M.; Al-Karadaghi, S.
The AAA(+) motor complex of subunits CobS and CobT of cobaltochelatase visualized by single particle electron microscopy
J. Struct. Biol.
167
227-234
2009
Brucella melitensis
brenda
Romao, C.V.; Ladakis, D.; Lobo, S.A.; Carrondo, M.A.; Brindley, A.A.; Deery, E.; Matias, P.M.; Pickersgill, R.W.; Saraiva, L.M.; Warren, M.J.
Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization
Proc. Natl. Acad. Sci. USA
108
97-102
2011
Archaeoglobus fulgidus, Salmonella enterica, Desulfovibrio vulgaris (Q72EC8)
brenda
Bali, S.; Rollauer, S.; Roversi, P.; Raux-Deery, E.; Lea, S.M.; Warren, M.J.; Ferguson, S.J.
Identification and characterization of the missing terminal enzyme for siroheme biosynthesis in alpha-proteobacteria
Mol. Microbiol.
92
153-163
2014
Paracoccus denitrificans, Paracoccus pantotrophus
brenda
Moore, S.J.; Mayer, M.J.; Biedendieck, R.; Deery, E.; Warren, M.J.
Towards a cell factory for vitamin B12 production in Bacillus megaterium: bypassing of the cobalamin riboswitch control elements
New Biotechnol.
31
553-561
2014
Priestia megaterium, Priestia megaterium DSM 319
brenda
Lobo, S.; Videira, M.; Pacheco, I.; Wass, M.; Warren, M.; Teixeira, M.; Matias, P.; Romao, C.; Saraiva, L.
Desulfovibrio vulgaris CbiKP cobaltochelatase evolution of a haem binding protein orchestrated by the incorporation of two histidine residues
Environ. Microbiol.
19
106-118
2017
Desulfovibrio vulgaris (Q72EC8), Desulfovibrio vulgaris DSM 644 (Q72EC8)
brenda