The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate

FEBS Letters

Volumn 331, Issue 1-2, 1993, Pages 123-128

  Noble, M E M ^a   Cleasby, A ^a   Johnson, L N ^a   Egmond, M R ^b   Frenken, L G J ^b  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNILEVER RESEARCH VLAARDINGEN   (Netherlands)

Author keywords

Catalytic triad; Crystal structure; Density modification; EC 3.1.1.3; Hydrolase fold; Triacylglycerol acylhydrolase

Indexed keywords

TRIACYLGLYCEROL LIPASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS;

AMINO ACID SEQUENCE; ASPARTIC ACID; CATALYSIS; CRYSTALLIZATION; LIPASE; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PSEUDOMONAS; SUPPORT, NON-U.S. GOV'T;

EID: 0027435346     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(93)80310-Q     Document Type: Article

References (28)

1. Ester synthesis in benzene by polyethylene glycol-modified lipase from Pseudomonas fragi 22.39B
2. The Xengen System VI.3
3. CCP4
4. The use of Sayre's equation with solvent flattening and histogram matching for phase extension and refinement of protein structures
5. Molecular Replacement
6. Improved Fourier coefficients for maps using phases from partial structures with errors
7. Improved methods for building protein models in electron density maps and the location of errors in these models
8. Mechanism of Activation of Eipolytic Enzymes
9. Pseudomonas glumae lipase: increased proteolytic stability by protein engineering.