BRENDA - Enzyme Database show
show all sequences of 4.6.1.17

Structure of a putative molybdenum-cofactor biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472)

Yoshida, H.; Yamada, M.; Kuramitsu, S.; Kamitori, S.; Acta Crystallogr. Sect. F 64, 589-592 (2008)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
Sulfurisphaera tokodaii
Crystallization (Commentary)
Crystallization
Organism
sitting-drop method, hanging-drop vapour-diffusion method, at room temperature
Sulfurisphaera tokodaii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sulfurisphaera tokodaii
Q975D5
-
-
Sulfurisphaera tokodaii 7
Q975D5
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
713624
Sulfurisphaera tokodaii
?
-
-
-
-
additional information
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
713624
Sulfurisphaera tokodaii 7
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
hexamer
-
Sulfurisphaera tokodaii
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
Sulfurisphaera tokodaii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
sitting-drop method, hanging-drop vapour-diffusion method, at room temperature
Sulfurisphaera tokodaii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
713624
Sulfurisphaera tokodaii
?
-
-
-
-
additional information
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
713624
Sulfurisphaera tokodaii 7
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
hexamer
-
Sulfurisphaera tokodaii
Other publictions for EC 4.6.1.17
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)
739551
Hover
Mechanism of pyranopterin ring ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
112
6347-6352
2015
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8
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6
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1
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1
1
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747097
Hover
Mechanistic investigation of ...
Escherichia coli
Biochemistry
54
7229-7236
2015
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1
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728595
Srivastava
Structural insights into putat ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
PLoS ONE
8
e58333
2013
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1
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4
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3
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726621
Srivastava
Overexpression, purification, ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
68
687-691
2012
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1
1
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1
2
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6
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1
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1
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1
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713617
Kanaujia
Structures of apo and GTP-boun ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Acta Crystallogr. Sect. D
66
821-833
2010
1
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1
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90
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1
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1
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713624
Yoshida
Structure of a putative molybd ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Acta Crystallogr. Sect. F
64
589-592
2008
1
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1
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5
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739638
Gray
Diverse splicing mechanisms fu ...
Homo sapiens
RNA
6
928-936
2000
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1
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1
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714888
Rieder
Rearrangement reactions in the ...
Escherichia coli
Eur. J. Biochem.
255
24-36
1998
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715420
Wuebbens
Investigation of the early ste ...
Escherichia coli
J. Biol. Chem.
270
1082-1087
1995
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