Information on EC 2.4.2.21 - nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
2.4.2.21
-
RECOMMENDED NAME
GeneOntology No.
nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole = nicotinate + alpha-ribazole 5'-phosphate
show the reaction diagram
single displacement mechanism
-
beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole = nicotinate + alpha-ribazole 5'-phosphate
show the reaction diagram
mechanism
-
beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole = nicotinate + alpha-ribazole 5'-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
adenosylcobalamin biosynthesis from cobyrinate a,c-diamide I
-
adenosylcobalamin biosynthesis from cobyrinate a,c-diamide II
-
adenosylcobalamin salvage from cobinamide I
-
adenosylcobalamin salvage from cobinamide II
-
Metabolic pathways
-
Porphyrin and chlorophyll metabolism
-
SYSTEMATIC NAME
IUBMB Comments
nicotinate-nucleotide:5,6-dimethylbenzimidazole phospho-D-ribosyltransferase
Also acts on benzimidazole, and the clostridial enzyme acts on adenine to form 7-alpha-D-ribosyladenine 5'-phosphate. The product of the reaction, alpha-ribazole 5'-phosphate, forms part of the corrin-biosynthesis pathway and is a substrate for EC 2.7.8.26, adenosylcobinamide-GDP ribazoletransferase [4]. It can also be dephosphorylated to form alpha-ribazole by the action of EC 3.1.3.73, alpha-ribazole phosphatase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5,6-dimethylbenzimidazole phosphoribosyltransferase
Q05603
-
ArsAB
F6MZ55 and F6MZ56
-
CobT
Q05603
-
N(1)-alpha-phosphoribosyltransferase
-
-
-
-
N1-alpha-phosphoribosyltransferase
-
-
-
-
nicotinate mononucleotide-dimethylbenzimidazole phosphoribosyltransferase
-
-
-
-
nicotinate ribonucleotide:benzimidazole (adenine) phosphoribosyltransferase
-
-
-
-
NN:DBI PRT
-
-
-
-
phosphoribosyltransferase, nicotinate mononucleotide-dimethylbenzimidazole
-
-
-
-
SoArsAB
F6MZ55 and F6MZ56
-
CAS REGISTRY NUMBER
COMMENTARY
37277-76-2
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,6-dimethylbenzimidazole + beta-nicotinate D-ribonucleotide
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole
show the reaction diagram
F6MZ55 and F6MZ56
-
-
-
?
5,6-dimethylbenzimidazole + beta-nicotinate D-ribonucleotide
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole
show the reaction diagram
-
-
-
-
?
beta-nicotinate D-ribonucleotide + 5(6)-nitrobenzimidazole
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-5(6)-nitrobenzimidazole
show the reaction diagram
-
-
-
-
?
beta-nicotinate D-ribonucleotide + 5,6-dichlorobenzimidazole
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-5,6-dichlorobenzimidazole
show the reaction diagram
-
-
-
-
?
beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole
show the reaction diagram
-
-
-
?
beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole
show the reaction diagram
-
-
-
-
?
beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole
show the reaction diagram
-
-
-
ir
beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole
show the reaction diagram
-
-
-
-
?
beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole
show the reaction diagram
P29935, -
-
-
-
?
NAD+ + 5,6-dimethylbenzimidazole
nicotinamide + alpha-5,6-dimethylbenzimidazole adenine dinucleotide
show the reaction diagram
-
step in the biosynthesis of coenzyme B12, nuceotide loop assembly NLA pathway overview
-
-
?
NAD+ + 5,6-dimethylbenzimidazole
NMN + alpha-5,6-dimethylbenzimidazole adenine dinucleotide
show the reaction diagram
-
-
alpha-5,6-dimethylbenzimidazole adenine dinucleotide product identification by mass spectrometry
-
?
nicotinamide nucleoside + benzimidazole
?
show the reaction diagram
-
-
-
-
ir
nicotinic acid mononucleotide + 4,5-dimethyl-1,2-phenylenediamine
nicotinate + ?
show the reaction diagram
-
-
-
-
?
nicotinic acid mononucleotide + adenine
nicotinate + ?
show the reaction diagram
-
-
-
-
?
nicotinic acid mononucleotide + adenine
7-alpha-D-ribofuranosyladenine 5'-phosphate + nicotinate
show the reaction diagram
-
-
-
?
nicotinic acid mononucleotide + adenine
7-alpha-D-ribofuranosyladenine 5'-phosphate + nicotinate
show the reaction diagram
-
-
-
?
nicotinic acid mononucleotide + benzimidazole
1-alpha-D-ribofuranosylbenzimidazole 5'-phosphate + nicotinate
show the reaction diagram
-
-
-
-
?
nicotinic acid mononucleotide + benzimidazole
1-alpha-D-ribofuranosylbenzimidazole 5'-phosphate + nicotinate
show the reaction diagram
-
-
-
-
?
nicotinic acid mononucleotide + benzimidazole
1-alpha-D-ribofuranosylbenzimidazole 5'-phosphate + nicotinate
show the reaction diagram
P29935, -
-
alpha-ribazole 5'-phosphate
?
nicotinic acid mononucleotide + benzimidazole
1-alpha-D-ribofuranosylbenzimidazole 5'-phosphate + nicotinate
show the reaction diagram
-
best substrate
-
ir
nicotinic acid mononucleotide + benzimidazole
1-alpha-D-ribofuranosylbenzimidazole 5'-phosphate + nicotinate
show the reaction diagram
-
highly specific for nicotinic acid mononucleotide
-
?
nicotinic acid mononucleotide + benzimidazole
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-benzimidazole
show the reaction diagram
-
-
-
-
?
nicotinic acid mononucleotide + benzimidazole
1-alpha-D-ribofuranosylbenzimidazole 5'-phosphate + nicotinic acid
show the reaction diagram
-
-
alpha-ribazole 5'-phosphate, intermediate for the lower ligand of cobalamin
?
nicotinic acid mononucleotide + guanine
nicotinate + ?
show the reaction diagram
-
-
-
-
?
nicotinic acid mononucleotide + histidine
nicotinate + ?
show the reaction diagram
-
-
-
-
?
nicotinic acid mononucleotide + imidazole
nicotinate + ?
show the reaction diagram
-
-
-
-
?
nicotinic acid nucleoside + benzimidazole
?
show the reaction diagram
-
-
-
-
ir
NMN + 5,6-dimethylbenzimidazole
nicotinamide + ?
show the reaction diagram
-
-
-
-
?
p-cresol + beta-nicotinate D-ribonucleotide
nicotinate + 4-hydroxyphenyl alpha-D-ribose 5-phosphate
show the reaction diagram
F6MZ55 and F6MZ56
-
-
-
?
p-cresol + beta-nicotinate D-ribonucleotide
nicotinate + 4-hydroxyphenyl alpha-D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
phenol + beta-nicotinate D-ribonucleotide
nicotinate + phenyl alpha-D-ribose 5-phosphate
show the reaction diagram
F6MZ55 and F6MZ56
-
-
-
?
phenol + beta-nicotinate D-ribonucleotide
nicotinate + phenyl alpha-D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole
nicotinate + N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole
show the reaction diagram
Q05603
-
-
-
?
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
not substrate: NAD, ribose 1-phosphate, ribose 5-phosphate, 2-methylbenzimidazole
-
-
-
additional information
?
-
F6MZ55 and F6MZ56
phloroglucinol is identified from an additive screen as a compound that dramatically improves the size, stability, and diffraction properties of the crystals. Subsequent structural studies show that phloroglucinol binds in the active site of ArsA
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD+ + 5,6-dimethylbenzimidazole
nicotinamide + alpha-5,6-dimethylbenzimidazole adenine dinucleotide
show the reaction diagram
-
step in the biosynthesis of coenzyme B12, nuceotide loop assembly NLA pathway overview
-
-
?
nicotinic acid mononucleotide + benzimidazole
1-alpha-D-ribofuranosylbenzimidazole 5'-phosphate + nicotinic acid
show the reaction diagram
-
-
alpha-ribazole 5'-phosphate, intermediate for the lower ligand of cobalamin
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.415
-
5,6-Dimethylbenzimidazole
-
pH 9.0, 37C, wild-type
0.5
-
benzimidazole
-
-
0.3
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G257A, at 37C; wild-type, at 37C
0.9
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G171D, at 37C
1
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G320D, at 37C
1.2
-
beta-nicotinate D-ribonucleotide
Q05603
mutant C160A, at 37C
2.2
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G257D, at 37C
0.000016
-
dimethylbenzimidazole
P29935
-
0.083
-
Nicotinic acid mononucleotide
P29935
-
0.3
-
Nicotinic acid mononucleotide
-
cosubstrate adenine
0.7
-
Nicotinic acid mononucleotide
-
cosubstrate benzimidazole
0.05
-
Phenol
-
pH 9.0, 37C, wild-type
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.6
-
5,6-Dimethylbenzimidazole
-
pH 9.0, 37C, wild-type
0.2
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G257D, at 37C; mutant G320D, at 37C
0.6
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G171D, at 37C
14
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G257A, at 37C
31
-
beta-nicotinate D-ribonucleotide
Q05603
mutant C160A, at 37C
38
-
beta-nicotinate D-ribonucleotide
Q05603
wild-type, at 37C
0.4
-
Phenol
-
pH 9.0, 37C, wild-type
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.9
-
5,6-Dimethylbenzimidazole
-
pH 9.0, 37C, wild-type
5026
0.1
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G257D, at 37C
7986
0.2
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G320D, at 37C
7986
0.7
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G171D, at 37C
7986
29
-
beta-nicotinate D-ribonucleotide
Q05603
mutant C160A, at 37C
7986
50
-
beta-nicotinate D-ribonucleotide
Q05603
mutant G257A, at 37C
7986
138
-
beta-nicotinate D-ribonucleotide
Q05603
wild-type, at 37C
7986
8
-
Phenol
-
pH 9.0, 37C, wild-type
15384
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0000007
-
-
substrate p-cresol, pH 9.0, 37C, mutant M87Q/I321S
0.0000024
-
-
substrate 5,6-dimethylbenzimidazole, pH 9.0, 37C, mutant M87Q/I321S
0.0000083
-
-
substrate p-cresol, pH 9.0, 37C, mutant I321S
0.0000142
-
-
substrate p-cresol, pH 9.0, 37C, mutant M87Q
0.0000167
-
-
substrate 5,6-dimethylbenzimidazole, pH 9.0, 37C, mutant I321S
0.0000376
-
-
substrate p-cresol, pH 9.0, 37C, wild-type
0.00016
-
-
substrate 5,6-dimethylbenzimidazole, pH 9.0, 37C, wild-type
0.000192
-
-
substrate 5,6-dimethylbenzimidazole, pH 9.0, 37C, mutant M87Q
0.0021
-
-
cell extract, substrate NMN
0.0025
-
-
cell extract, substrate NAD+
0.035
-
-
cell extract, substrate beta-nicotinate D-riboadenosine
0.1
-
Q05603
mutant G257D, at 37C
0.2
-
Q05603
mutant G320D, at 37C
0.5
-
Q05603
mutant G171D, at 37C
11
-
Q05603
mutant G257A, at 37C
25
-
Q05603
mutant C160A, at 37C
30
-
Q05603
wild-type, at 37C
additional information
-
P29935
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.6
9.2
-
nicotinic acid mononucleotide + adenine or benzimidazole
8.6
-
-
assay at
9
-
-
assay at
additional information
-
-
assay at pH 7.0 or pH 10.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.3
9.7
-
pH 7.3: about 60% of maximum activity, pH 9.7: about 90% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
P29935
assay at
37
-
-
assay at
PDB
SCOP
CATH
ORGANISM
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
71000
-
P29935
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
P29935
2 * 35000, SDS-PAGE
dimer
-
2 * alpha, Glu317 is catalytic site, x-ray structure
heterodimer
-
ArsA and ArsB. Only the active site in ArsA is occupied by substrate. Analysis of the ArsB active site identified an arginyl side chain that may block access to the site
heterodimer
-
functional as a heterodimer, 1 * 36650 (ArsA) + 1 * 36180 (ArsB), SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with different substrate analogs, reaction pathway
-
in complex with substrate and with reaction product
-
phloroglucinol is identified from an additive screen as a compound that dramatically improves the size, stability, and diffraction properties of the crystals. Subsequent structural studies show that phloroglucinol binds in the active site of ArsA; the three-dimensional crystal structure of Sporomusa ovata ArsAB in its substrate-free form (2.1 A), and in complex with DMB (1.5 A), p-cresol (2.1 A), phloroglucinol (1.6 A), and phenol (2.4 A) is reported. Only the active site in ArsA is occupied by substrate. Analysis of the ArsB active site identified an arginyl side chain that may block access to the site
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, 0.01 M potassium phosphate buffer, pH 6.8, 0.005 M DTT, 10% ethylene glycol, several months
-
-80C, 50 mM Tris-HCl buffer, pH 7.5, 3 M glycerol
Q05603
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by gel filtration
Q05603
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
wild-type and mutants cloned into vector pSU18 or vector pT7-5. Plasmids carrying wild-type or mutant cobT alleles introduced into strain JE2607 (cobT cobB recA) or strain JE2423 (cobT recA). Plasmids encoding mutant cobT alleles under the control of the T7 promoter of vector pT7-5 transformed into strain JE2017 and overexpressed
Q05603
gene cobT, comparison with homologues
-
expressed in Escherichia coli
F6MZ55 and F6MZ56
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C160A
Q05603
loss of catalytic efficiency by 79%. Renders the enzyme 5fold less efficient than wild-type. Displays no discernible growth defect in no-carbon essential (NCE) medium containing dicyanocobinamide and glycerol or ethanolamine relative to that of a strain that synthesizes wild-type
G171D
Q05603
loss of catalytic efficiency by more than 99%, has less affinity for 5,6-dimethylbenzimidazole. Retains activity to support growth, but only when 5,6-dimethylbenzimidazole is present in the medium. Does not support the growth of strain JE2423 on ethanolamine in medium that contains dicyanocobinamide but lacks 5,6-dimethylbenzimidazole
G171D/M325A
Q05603
requires cobalamin for growth regardless of the carbon source used
G257A
Q05603
loss of catalytic efficiency by 64%
G257D
Q05603
loss of catalytic efficiency by more than 99%, has less affinity for 5,6-dimethylbenzimidazole. Does not respond to 5,6-dimethylbenzimidazole and requires cobalamin to grow. Does not support the growth of strain JE2423 on ethanolamine in medium that contains dicyanocobinamide but lacks 5,6-dimethylbenzimidazole
G257D/P12G
Q05603
is cobalamin auxotroph on glycerol or ethanolamine. P12G does not alter the effect of the G257D mutation
G320D
Q05603
loss of catalytic efficiency by more than 99%, is unstable, retains activity to support growth, but only when 5,6-dimethylbenzimidazole is present in the medium. Does not support the growth of strain JE2423 on ethanolamine in medium that contains dicyanocobinamide but lacks 5,6-dimethylbenzimidazole
H289A
Q05603
counteracts the effect of the G320D substitution
M325A
Q05603
grows in the absence of exogenous 5,6-dimethylbenzimidazole, albeit at a rate slower than that of a strain making wild-type. Addition of 5,6-dimethylbenzimidazole to the medium allows the strain making M325A to grow as fast as a strain making wild-type
P12G
Q05603
does not require exogenous 5,6-dimethylbenzimidazole for growth on glycerol or ethanolamine
I321S
-
specific activity with p-cresol and 5,6-dimethylbenzimidazole decreased
M87Q
-
effect of the M87Q mutation is most pronounced with respect to phenolic specificity, as the specific activity with p-cresol drops by 2.6fold while a 1.2fold increase in activity with 5,6-dimethylbenzimidazole is observed
M87Q/I321S
-
specific activity with p-cresol and 5,6-dimethylbenzimidazole highly decreased