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Literature summary for 1.4.1.1 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)

Cloned (Comment) Organism
-
Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
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]

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

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WQB1
-
-
Mycobacterium tuberculosis H37Rv P9WQB1
-
-

Purification (Commentary)

Purification (Comment) Organism
using affinity chromatography Mycobacterium tuberculosis

Storage Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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+
-
?
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

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

Synonyms

Synonyms Comment Organism
alanine dehydrogenase
-
Mycobacterium tuberculosis
ALD
-
Mycobacterium tuberculosis
MtbALD
-
Mycobacterium tuberculosis
Rv2780
-
Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Mycobacterium tuberculosis