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Literature summary for 1.2.1.88 extracted from

  • Luo, M.; Singh, R.K.; Tanner, J.J.
    Structural determinants of oligomerization of delta(1)-pyrroline-5-carboxylate dehydrogenase: identification of a hexamerization hot spot (2013), J. Mol. Biol., 425, 3106-3120.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermus thermophilus
expression in Escherichia coli Deinococcus radiodurans
expression in Escherichia coli Halalkalibacterium halodurans
expression in Escherichia coli Bacillus licheniformis

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Bacillus licheniformis
mutants R100A crystallizes in the same lattice as wild-type, mutant R100A/K104A/R111A crystaLLIZES IN space group P1 Thermus thermophilus
space group P21 with eight molecules in the asymmetric unit Halalkalibacterium halodurans

Protein Variants

Protein Variants Comment Organism
K104A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer Thermus thermophilus
R100A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer Thermus thermophilus
R100A/K104A/R111A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer Thermus thermophilus
R102A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer Deinococcus radiodurans
R111A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer Thermus thermophilus
R153A mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer Thermus thermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
119000
-
dynamic light scattering Halalkalibacterium halodurans
119000
-
dynamic light scattering Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis Q65NN2
-
-
Bacillus licheniformis DSM 13 Q65NN2
-
-
Deinococcus radiodurans Q9RW56
-
-
Deinococcus radiodurans DSM 20539 Q9RW56
-
-
Halalkalibacterium halodurans Q9K9B2
-
-
Halalkalibacterium halodurans DSM 18197 Q9K9B2
-
-
Thermus thermophilus Q72IB9
-
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 Q72IB9
-
-

Subunits

Subunits Comment Organism
dimer crystallization data Bacillus licheniformis
dimer dynamic light scattering and crystallization data Halalkalibacterium halodurans
hexamer protein exists primarily as a trimer-of-dimers hexamer in solution, small-angle X-ray scattering and crystallization data Thermus thermophilus
hexamer protein exists primarily as a trimer-of-dimers hexamer in solution, small-angle X-ray scattering and crystallization data Deinococcus radiodurans

Synonyms

Synonyms Comment Organism
DR_0813
-
Deinococcus radiodurans