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Enzyme Nomenclature
Information on EC 4.99.1.3 - sirohydrochlorin cobaltochelatase
Word Map on EC 4.99.1.3
- 4.99.1.3
- protoporphyrin
- tetrapyrrole
-
uroporphyrinogen
- megaterium
- typhimurium
- precorrin-2
-
atp-independent
-
primordial
-
histidine-rich
-
ferrochelation
- epr
-
sirohaem
-
dehydrogenation
- chlorophyll
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Specify your search results
The expected taxonomic range for this enzyme is: Archaea, Bacteria
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EC NUMBER 
COMMENTARY 
4.99.1.3
-
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RECOMMENDED NAME
GeneOntology No.
sirohydrochlorin cobaltochelatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cobalt-sirohydrochlorin + 2 H+ = sirohydrochlorin + Co2+
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
cobalt-sirohydrochlorin cobalt-lyase (sirohydrochlorin-forming)
This enzyme is a type II chelatase, being either a monomer (CbiX) or a homodimer (CibK) and being ATP-independent. CbiK from Salmonella enterica uses precorrin-2 as the substrate to yield cobalt-precorrin-2. The enzyme contains two histidines at the active site that are thought to be involved in the deprotonation of the tetrapyrrole substrate as well as in metal binding. CbiX from Bacillus megaterium inserts cobalt at the level of sirohydrochlorin (factor-II) rather than precorrin-2.
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CAS REGISTRY NUMBER
COMMENTARY
81295-49-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
a cbiX-deficient mutant is unable to respire anaerobically on nitrate
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
precorrin-2 + Co2+
cobalt-precorrin-2 + H+
-
-
-
?
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+
-
-
-
?
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+
-
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 + 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
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
Methanobacter thermoautotrophicum
-
cobalamin biosynthetic pathway
-
?
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+
-
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+
-
-
-
?
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+
-
-
-
?
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
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
precorrin-2 + Co2+
Co-precorrin-2 + H+
-
tetrapyrrole biosynthesis, formation of tetrapyrrole cofactors
-
?
sirohydrochlorin + Fe2+
iron-sirohydrochlorin + 2 H+
Q72CB8, Q72EC8
-
-
-
?
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+
-
biosynthesis of vitamin B12
-
?
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.004
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
CbiKc, the isozyme lacks an N-terminal transit peptide; enzyme may be involved in cytoplasmic cobalamin biosynthesis
-
CbiKc, the isozyme lacks an N-terminal transit peptide; enzyme may be involved in cytoplasmic cobalamin biosynthesis
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14000
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
40000
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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
-
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
tetramer
additional information
-
the molecules are arranged in a two-tiered ring structure with the six subunits in each ring organized as a trimer of dimers, subunits CobS and CobT form a chaperone-like complex. Homology modelling of subunit CobS, overview
?
x * 28000, SDS-PAGE and calculated, mature protein; x * 31000, PAGE and calculated, mature protein; x * 31000, recombinant enzyme, SDS-PAGE
?
-
x * 28000, SDS-PAGE and calculated, mature protein; x * 31000, PAGE and calculated, mature protein; x * 31000, recombinant enzyme, SDS-PAGE
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
additional information
proteolytic modification
processing of 28 amino acid signal peptide
proteolytic modification
-
processing of 28 amino acid signal peptide
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using the sitting drop vapor diffusion technique in 96-well plates, in two different crystal forms consisting of a central mixed b-sheet flanked by four alpha helices
hanging drop vapor diffusion method, using 100 mM Tris-HCl. pH 8.5, containing 2.0 M ammonium sulfate
using the sitting drop vapor diffusion technique in 96-well plates, in two different crystal forms consisting of a central mixed b-sheet flanked by four alpha helices
hexagonal crystals are grown using the hanging-drop method, crystals are in space group P6(3)22 with cell dimensions a = b = 128.08 A, c = 85.44 A
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by using a metal chelating affinity column charged with Ni2+ or a chelating Sepharose-column charged with Co2+
recombinant His-tagged wild-type isozyme and mutant DELTA28DVU0650 from Escherichia coli by nickel affinity chromatography, dialysis, anion exchange chromatography and gel filtration; recombinant His-tagged wild-type isozyme from Escherichia coli by nickel affinity chromatography, dialysis, anion exchange chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; expression in Escherichia coli; gene DVU0650, DNA and amino acid sequence determination and analysis, expression of wild-type enzyme and mutant DELTA28DVU0650 in Escherichia coli as His-tagged proteins, complementation of Escherichia coli cysG mutant strain by DELTA28CbiKP; gene DVU1365, DNA and amino acid sequence determination and analysis, expression of wild-type enzyme in Escherichia coli as His-tagged protein, complementation of Escherichia coli cysG mutant strain by CbiKC
genes cobN, cobS and cobT, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3)
-
overexpressed in Escherichia coli BL21(DE3)pLys cells by cloning the gene into pET14b
-
overexpression in Escherichia coli as non His-tagged protein, as His-tagged protein fusion protein and as selenomethionine-substituted protein
overexpression in siroheme deficient Escherichia coli after random in vitro gene sequence rearrangements in order to screen the generated library for Escherichia coli cells that are able to insert both cobalt and to a lesser extend iron into its tetrapyrrole substrate sirohydrochlorin
overproduced in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
10 nM exogenous cobalt decreases the levels of the enzyme 13fold
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H192A
double mutation in M518 mutant; double mutation in M51 mutant
H145A/H207A
-
site-directed mutagenesis
additional information
additional information
CbiKc gene is able to complement an Escherichia coli cysG mutant; CbiKp gene is able to complement an Escherichia coli cysG mutant; 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; CbiKp gene is able to complement an Escherichia coli cysG mutant; 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; CbiKp gene is able to complement an Escherichia coli cysG mutant; 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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