BRENDA - Enzyme Database

How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum

Tollinger, M.; Konrat, R.; Hilbert, B.H.; Marsh, E.N.; Krautler, B.; Structure 15, 1021-1033 (1998)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
5.4.99.1
-
Clostridium tetanomorphum
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
5.4.99.1
14800
-
2 * 14800, B12-binding component S, + 2 * 53700, component E
Clostridium tetanomorphum
5.4.99.1
53700
-
2 * 14800, B12-binding component S, + 2 * 53700, component E
Clostridium tetanomorphum
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
5.4.99.1
Clostridium tetanomorphum
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.99.1
L-Glu
-
3464
Clostridium tetanomorphum
threo-3-Methylaspartate
-
3464
Clostridium tetanomorphum
-
Subunits
EC Number
Subunits
Commentary
Organism
5.4.99.1
tetramer
2 * 14800, B12-binding component S, + 2 * 53700, component E
Clostridium tetanomorphum
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
5.4.99.1
Cobalamin
dependent on; the major part of component S is preorganized for vitamin B12 binding, but the B12-binding site itself is only partially formed. Upon binding B12, important elements of the binding site appear to become structured, including an alpha-helix that forms one side of the cleft accomodating the nucleotide 'tail' of the cofactor
Clostridium tetanomorphum
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
5.4.99.1
Cobalamin
dependent on; the major part of component S is preorganized for vitamin B12 binding, but the B12-binding site itself is only partially formed. Upon binding B12, important elements of the binding site appear to become structured, including an alpha-helix that forms one side of the cleft accomodating the nucleotide 'tail' of the cofactor
Clostridium tetanomorphum
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
5.4.99.1
-
Clostridium tetanomorphum
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
5.4.99.1
14800
-
2 * 14800, B12-binding component S, + 2 * 53700, component E
Clostridium tetanomorphum
5.4.99.1
53700
-
2 * 14800, B12-binding component S, + 2 * 53700, component E
Clostridium tetanomorphum
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.99.1
L-Glu
-
3464
Clostridium tetanomorphum
threo-3-Methylaspartate
-
3464
Clostridium tetanomorphum
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
5.4.99.1
tetramer
2 * 14800, B12-binding component S, + 2 * 53700, component E
Clostridium tetanomorphum