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Literature summary for 3.4.11.15 extracted from

  • Munih, P.; Moulin, A.; Stamper, C.C.; Bennett, B.; Ringe, D.; Petsko, G.A.; Holz, R.C.
    X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica (2007), J. Inorg. Biochem., 101, 1099-1107.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
x-ray crystal structure of the Co(II)-loaded form ([CoCo(AAP)]) is solved to 2.2 A resolution. [CoCo(AAP)] folds into an alpha/beta globular domain with a twisted beta-sheet hydrophobic core sandwiched between alpha-helices, identical to [ZnZn(AAP)]. Tris(hydroxymethyl)aminomethane coordinates to the dinuclear Co(II) active site of AAP with one of the Tris hydroxyl oxygen atoms (O4) forming a single oxygen atom bridge between the two Co(II) ions. This is the only Tris atom coordinated to the metals with Co1-O and Co2-O bonds distances of 2.2 and 1.9 A, respectively. Each of the Co(II) ions resides in a distorted trigonal bipyramidal geometry Vibrio proteolyticus

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ for spectroscopic studies the enzyme containing magnetically and spectroscopically silent Zn(II) ion is substituted with Co(II) Vibrio proteolyticus
Zn2+ native protein Vibrio proteolyticus

Organism

Organism UniProt Comment Textmining
Vibrio proteolyticus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-leucine p-nitroanilide + H2O
-
Vibrio proteolyticus L-leucine + p-nitroaniline
-
?

Synonyms

Synonyms Comment Organism
AAP
-
Vibrio proteolyticus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
-
Vibrio proteolyticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Vibrio proteolyticus