BRENDA - Enzyme Database show
show all sequences of 2.1.1.107

Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis

Vevodova, J.; Graham, R.M.; Raux, E.; Schubert, H.L.; Roper, D.I.; Brindley, A.A.; Ian Scott, A.; Roessner, C.A.; Stamford, N.P.; Elizabeth Stroupe, M.; Getzoff, E.D.; Warren, M.J.; Wilson, K.S.; J. Mol. Biol. 344, 419-433 (2004)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
enzyme topology diagramm
Pseudomonas denitrificans (nomen rejiciendum)
Engineering
Amino acid exchange
Commentary
Organism
D47N
binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1
Pseudomonas denitrificans (nomen rejiciendum)
F106A
considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity
Pseudomonas denitrificans (nomen rejiciendum)
L49A
binds about half the quantity of S-adenosyl-L-methionine compared with wild-type, reaction products are oxidised forms of both precorrin-1 and precorrin-2
Pseudomonas denitrificans (nomen rejiciendum)
M184A
slight enzymic activity
Pseudomonas denitrificans (nomen rejiciendum)
T130A
considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine
Pseudomonas denitrificans (nomen rejiciendum)
Y183A
considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity
Pseudomonas denitrificans (nomen rejiciendum)
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas denitrificans (nomen rejiciendum)
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
crystallization data
Pseudomonas denitrificans (nomen rejiciendum)
Crystallization (Commentary) (protein specific)
Crystallization
Organism
enzyme topology diagramm
Pseudomonas denitrificans (nomen rejiciendum)
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D47N
binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1
Pseudomonas denitrificans (nomen rejiciendum)
F106A
considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity
Pseudomonas denitrificans (nomen rejiciendum)
L49A
binds about half the quantity of S-adenosyl-L-methionine compared with wild-type, reaction products are oxidised forms of both precorrin-1 and precorrin-2
Pseudomonas denitrificans (nomen rejiciendum)
M184A
slight enzymic activity
Pseudomonas denitrificans (nomen rejiciendum)
T130A
considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine
Pseudomonas denitrificans (nomen rejiciendum)
Y183A
considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity
Pseudomonas denitrificans (nomen rejiciendum)
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
crystallization data
Pseudomonas denitrificans (nomen rejiciendum)
Other publictions for EC 2.1.1.107
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
733749
Wang
Engineering uroporphyrinogen I ...
Hordeum vulgare
Enzyme Microb. Technol.
61-62
1-6
2014
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734345
Wang
Coupled selection of protein s ...
Escherichia coli
J. Biotechnol.
186
169-174
2014
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747676
Wang
Engineering uroporphyrinogen ...
Hordeum vulgare
Enzyme Microb. Technol.
61-62
1-6
2014
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714579
Vannini
Cloning and heterologous expre ...
Lactobacillus reuteri, Lactobacillus reuteri CRL 1098
Biotechnol. Lett.
33
1625-1632
2011
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4
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1
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1
1
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719948
Storbeck
Crystal structure of the heme ...
Pseudomonas aeruginosa
J. Biol. Chem.
286
26754-26767
2011
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1
9
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696120
Lobo
Functional characterization of ...
Desulfovibrio vulgaris
Biochem. J.
420
317-325
2009
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1
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1
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2
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703663
Storbeck
The Pseudomonas aeruginosa nir ...
Pseudomonas aeruginosa
FEBS J.
276
5973-5982
2009
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1
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1
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706702
Araya
Cloning, purification and char ...
Geobacillus stearothermophilus, Geobacillus stearothermophilus V
Res. Microbiol.
160
125-133
2009
-
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1
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1
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2
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5
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1
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1
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1
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676956
Fan
Maize uroporphyrinogen III met ...
Zea mays
Protein Expr. Purif.
46
40-46
2006
-
1
1
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1
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3
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3
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660612
Rehse
Structure of a closed-form uro ...
Thermus thermophilus
Acta Crystallogr. Sect. D
61
913-919
2005
-
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1
1
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662638
Vevodova
Structure/function studies on ...
Pseudomonas denitrificans (nomen rejiciendum)
J. Mol. Biol.
344
419-433
2004
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1
6
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485092
Raux
-
The role of Saccharomyces cere ...
Escherichia coli, Pseudomonas denitrificans (nomen rejiciendum), Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium
Biochem. J.
338
701-708
1999
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485091
Woodcock
-
Effect of mutations in the tra ...
Escherichia coli
Biochem. J.
330
121-129
1998
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7
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7
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485090
Leustek
Siroheme biosynthesis in highe ...
Arabidopsis thaliana
J. Biol. Chem.
272
2744-2752
1997
-
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1
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1
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1
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3
2
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5
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1
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1
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4
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1
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2
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1
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4
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485089
Sakakibara
Isolation and characterization ...
Zea mays
Plant J.
10
883-892
1996
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1
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4
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485087
Sattler
Cloning, sequencing, and expre ...
Propionibacterium freudenreichii
J. Bacteriol.
177
1564-1569
1995
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1
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1
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485088
Chou
Reddish Escherichia coli cells ...
Geobacillus stearothermophilus
Biosci. Biotechnol. Biochem.
59
1817-1824
1995
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1
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727722
Blanche
Purification, characterization ...
Methanobacterium ivanovii
J. Bacteriol.
173
4637-4645
1991
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1
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1
1
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4
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485083
Warren
-
Uroporpyrinogen III methylase ...
Escherichia coli
J. Am. Chem. Soc.
112
5343-5345
1990
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485084
Warren
The Escherichia coli cysG gene ...
Escherichia coli
Biochem. J.
265
725-729
1990
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1
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3
1
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1
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485086
Crouzet
Nucleotide sequence of a Pseud ...
Pseudomonas denitrificans (nomen rejiciendum)
J. Bacteriol.
172
5968-5979
1990
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1
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2
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2
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485085
Blanche
Purification and characterizat ...
Pseudomonas denitrificans (nomen rejiciendum)
J. Bacteriol.
171
4222-4231
1989
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1
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3
5
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1
2
1
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2
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1
1
8
1
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1
1
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1
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1
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3
1
5
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1
2
1
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1
1
8
1
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1
1
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