Protein engineering from a bioindustrial point of view

422 Protein engineering
computer-aided design and structural mutants. Protein Eng
1996, 9:507-51 Z
The combination of modeling with site-directed mutagenesis allows a de-
tailed picture of the reaction mechanism of a lipase to be developed. Many
similarities with serine protease are seen. The added feature of inter-facial
activation is not covered here.
47. Brady I, Brzozowsi A, Derwenda Z, Dobson G, Tolley S,
Turkenburg J, Christiansen L, Huge-Jensen B, Norskov L, Thim L,
Menge U: A serine protease triad forms the catalytic centre of
a triacylglycerol lipase. Nature 1990, 343:767-770.
46. Martinelle M, Holmquiest M, Clausen IG, Patkar S, Svensen A,
. Huh K: The role of glu67 and trp89 in the lid of Humicola
lanuginose lipase. Protein Eng 1996, 9519-524.
This provides a complementary study to reference [471 focusing more on
mutations affecting enzyme-substrate interactions.
49.
50.
51.
52.
Svensen A: Protein engineering of microbial lipases with
industrial interest In Enzyme Technology for industrial
Applications. Edited by Savage L. Southbourough MA: IBC
Biomedical Library Series; 1996:91-97.
Pedersen S, Lange KN, Nissen AM: Novel industrial enzyme
applications. Ann NY Acad Sci 1995, 750:376-390.
Reinikainen T, Teleman 0, Teeri lT: Effects of pH and high ionic
strength on the adsorption and activity of native and mutated
Cellobiohydrolase I from Trichoderma reesei. Proteins 1995,
22:392-403.
53. Koivula A, Reinikainen T, Ruohonen L, Valkeajawi A, Claeyssens
. M, Teleman 0, Kleywegt GJ, Szardenings M, Rouvinen J,
Jones TA, Teeri lT: The active site of Trichoderma reesei
cellobiohydrolase II: the role of tyrosine 169. Protein Eng 1996,
9:691-699.
This paper provides a look at the more intimate details of the catalytic chem-
istry of cellobiohydrolase II from Trchoderma reesei. Together references
[51] and [!%*I provide a good perspective of the global and local variables
important in cellulase catalysis.
54. Jeffries TW: Enzyme technology for pulp bleaching and
deinking. In Enzyme Technology for industrial Applications Edited
by Savage L. Southbourough MA: IBC Biomedical Library Series;
1996:61-97.
55. Jeffries TW: Biochemistry and genetics of microbial xyianases.
Curr Opin Biotechnol 1996, 71337-342.
;his paper provides a description of the major xylanase families, the im-
portant regions in substrate binding and catalysis, data on stability and pH
dependence of activity, as well as some discussion of comercial applications.
As such it provides a good starting point to gain a perspective on microbial
xylanases.
56. Lawson SL, Wakarchuk WW, Withers SG: Effects of both
. shortening and lengthening the active site nucleophile of
Bacillus circu/ans xylanase on catalytic activity. Biochemistry
1996, 35:lOll O-l 0116.
Linder M, Salovuori I, Ruohonen L, Teeri TT: Characterization The hydrolysis of glycosidase bonds can proceed by two mechanisms that
of a double cellulose-binding domain. I Biol Chem 1996, are critically dependent upon the distance separating the carboxyl groups. In
271:21266-21272.
this work, the catalytic consequences of changing this distance are explored.