1992
DOI: 10.1016/0022-2836(92)90593-9
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Crystallization and preliminary X-ray study of a lipase from Pseudomonas glumae

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Cited by 25 publications
(5 citation statements)
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“…A reason for these structural changes may be the different crystallization conditions of the two lipases. PGL was crystallized at pH 9 (Cleasby et al, 1992), whereas CVL was crystallized at pH 6.4 (Lang et al, 1994). Biochemical investigations (Prazeres et al, 1992;Deveer, 1992) have shown a bell-shaped pH activity profile between pH 5.5 and 9 with an optimum at pH 7.0 to 7.5 for the enzymes.…”
Section: Comparison With the Three-dimensional Structure Of The Lipasmentioning
confidence: 99%
“…A reason for these structural changes may be the different crystallization conditions of the two lipases. PGL was crystallized at pH 9 (Cleasby et al, 1992), whereas CVL was crystallized at pH 6.4 (Lang et al, 1994). Biochemical investigations (Prazeres et al, 1992;Deveer, 1992) have shown a bell-shaped pH activity profile between pH 5.5 and 9 with an optimum at pH 7.0 to 7.5 for the enzymes.…”
Section: Comparison With the Three-dimensional Structure Of The Lipasmentioning
confidence: 99%
“…So it's important to dissolve the protein at a suitable concentration. The tendency of lipases to aggregate has been reported by others (Cleasby et al, 1992;Duenhaupt et al, 1992;Lesuisse et al, 1993). Effects of temperature and pH on enzyme activity and stability Lipase activity assays were carried out at 30-80 °C and we found the optimum temperature of the S31 lipase is between 65 and 70 °C (Fig.…”
Section: Purification Of S31 Lipase and Determination Of Its Moleculamentioning
confidence: 86%
“…The deduced protein sequence of the S31 lipase gene was aligned with those from P. cepacia (M58494), B. cenocepacia (EAM08623), P. aeruginosa (AY682924), and P. glumae (Cleasby et al, 1992). Sequence identity between LipA from S31 and those from P. cepacia, P. glumae and P. aeruginosa is 96, 80 and 35%, respectively.…”
Section: Gene Cloning Of S31 Lipasementioning
confidence: 99%
“…Considerable information is available for the lipases (EC 3.1.1.3). X-ray structures of the lipases from P. gtumae (Cleasby et at., 1992), P. fluorescens , P. aeruginosa (Misset et at., 1994), Pseudomonas sp. (Kordel et at., 1991), and P. cepacia (Kim et ai., 1992) binding pocket of lipase (active site modeling), the 'proper' enzyme for a given substrate can be selected.…”
Section: Protein Engineeringmentioning
confidence: 99%