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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+
-
-
-
-
?
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+
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+
-
-
-
?
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+
-
-
-
?
sirohydrochlorin + Co2+
cobaltsirohydrochlorin + H+
-
cobalamin biosynthesis
-
?
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+
-
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 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
-
?
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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+
Q72CB8, Q72EC8
-
-
-
?
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+
Q72CB8, Q72EC8
a step involved in the vitamin B12 biosynthesis
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
Q72CB8, Q72EC8
a step involved in the vitamin B12 biosynthesis
-
-
?
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+
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+
-
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
-
?
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 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

?
-
Q72CB8
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
-
additional information
?
-
Q72EC8
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
-
additional information
?
-
Q72CB8
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
-
additional information
?
-
Q72EC8
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
-
additional information
?
-
Q72CB8
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
-
additional information
?
-
Q72EC8
CbiKC is likely to be the enzyme associated with cytoplasmic cobalamin biosynthesis
-
-
-
additional information
?
-
Q72CB8
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
-
additional information
?
-
Q72EC8
CbiKP is periplasmic located and possibly associated with an iron transport system
-
-
-
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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
31000
x * 31000, PAGE and calculated, mature protein; x * 31000, recombinant enzyme, SDS-PAGE
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
137000
-
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
14000

Methanobacter thermoautotrophicum
-
gene-predicted molecular mass
14000
-
gene-predicted molecular mass
40000

Methanobacter thermoautotrophicum
-
gel filtration
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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
Methanobacter thermoautotrophicum, Methanosarcina barkeri, Methanosarcina barkeri Fusaro
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
Bacillus 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
Bacillus megaterium, Clostridioides difficile, Clostridium acetobutylicum, no activity in Bacillus subtilis, no activity in eukaryota, Porphyromonas gingivalis, Pseudomonas aeruginosa, Rhodobacter sphaeroides, Salmonella enterica subsp. enterica serovar Typhimurium
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
Bacillus megaterium, Bacillus megaterium DSM 509, Synechocystis sp.
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, Desulfovibrio vulgaris (Q72EC8), Salmonella enterica
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
Bacillus megaterium, Bacillus megaterium DSM 319
brenda