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Literature summary extracted from

  • Tripathi, S.; Ramachandran, R.
    Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures "open" and "closed" enzyme conformations (2008), Proteins Struct. Funct. Genet., 72, 1089-1095.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.1
-
 Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.1.1 using the hanging-drop method crystal structures of the apo enzyme as also a ternary complex with NAD and pyruvate is reported. Each chain of the enzyme can be divided into catalytic and NAD-binding domains, respectively. The individual subunits associate into a hexamer with the catalytic domains on the outside as observed in the apo and holo enzyme crystals. The structures have captured open and closed conformations of the enzyme and clarify that a domain rearrangement step must take place during the reaction as opposed to alterations in intersubunit interactions Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.1 40000
-
 SDS-PAGE Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.1 Mycobacterium tuberculosis P9WQB1
-
-
1.4.1.1 Mycobacterium tuberculosis H37Rv P9WQB1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.1 using affinity chromatography Mycobacterium tuberculosis

Storage Stability

EC Number Storage Stability Organism
1.4.1.1 4°C, stable up to 1 week without degradation Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.1 pyruvate + NH3 + NADH the structural analysis leads to the identification of a water molecule which is hydrogen bonded to the active site His 96 and probably drives the conversion of the iminopyruvate intermediate to a carbinolamine Mycobacterium tuberculosis L-alanine + H2O + NAD+
-
 ?
1.4.1.1 pyruvate + NH3 + NADH the structural analysis leads to the identification of a water molecule which is hydrogen bonded to the active site His 96 and probably drives the conversion of the iminopyruvate intermediate to a carbinolamine Mycobacterium tuberculosis H37Rv L-alanine + H2O + NAD+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.1.1 hexamer 6 * 40000 Da, gel filtration and crystal structure Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
1.4.1.1 alanine dehydrogenase
-
 Mycobacterium tuberculosis
1.4.1.1 ALD
-
 Mycobacterium tuberculosis
1.4.1.1 MtbALD
-
 Mycobacterium tuberculosis
1.4.1.1 Rv2780
-
 Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.1 NAD+
-
 Mycobacterium tuberculosis