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Literature summary for 3.4.19.1 extracted from

  • Zhang, H.F.; Zheng, B.S.; Peng, Y.; Lou, Z.Y.; Feng, Y.; Rao, Z.H.
    Expression, purification and crystal structure of a truncated acylpeptide hydrolase from Aeropyrum pernix K1 (2005), Acta Biochim. Biophys. Sin., 37, 613-617.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
a truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal is cloned and expressed in Escherichia coli Aeropyrum pernix K1

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method, 2.5 A resolution, space group: P2(1)2(1)2(1), unit cell parameters: a = 63.1 A, b = 102.3 A, c = 163.9 A, truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal is cloned and expressed in Escherichia coli Aeropyrum pernix K1

Protein Variants

Protein Variants Comment Organism
DELTA1-21 optimal temperature of a truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal is decreased by 15°C Aeropyrum pernix K1

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix K1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Aeropyrum pernix K1

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
75
-
truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal Aeropyrum pernix K1
90
-
wild-type enzyme Aeropyrum pernix K1