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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003920naa a2200445 4500
001oai:DiVA.org:kth-7587
003SwePub
008071107s2004 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-75872 URI
0247 a https://doi.org/10.1021/bi049453x2 DOI
040 a (SwePub)kth
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Master, Emmau KTH,Bioteknologi4 aut0 (Swepub:kth)u13skjyk
2451 0a Recombinant Expression and Enzymatic characterization of PttCel9A, a KOR homologue from Populus tremula x tremuloides
264 c 2004-07-15
264 1b American Chemical Society (ACS),c 2004
338 a print2 rdacarrier
500 a QC 20100802 QC 20110927
520 a PttCel9A is a membrane-bound, family 9 glycosyl hydrolase from Populus tremula x tremuloides that is upregulated during secondary cell wall synthesis. The catalytic domain of PttCel9A, Delta(1-105)PttCel9A, was purified, and its activity was compared to TfCel9A and TfCel9B from Thermobifida fusca. Since aromatic amino acids involved in substrate binding at subsites -4, -3, and -2 are missing in PttCel9A, the activity of TfCel9A mutant enzymes W256S, W209A, and W313G was also investigated. Delta(1-105)PttCel9A hydrolyzed a comparatively narrow range of polymeric substrates, and the preferred substrate was (carboxymethyl)cellulose 4M. Moreover, Delta(1-105)PttCel9A did not hydrolyze oligosaccharides shorter than cellopentaose, whereas TfCel9A and TfCel9B hydrolyzed cellotetraose and cellotriose, respectively. These data suggest that the preferred substrates of PttCel9A are long, low-substituted, soluble cellulosic polymers. At 30degreesC and pH 6.0, the k(cat) for cellohexaose of Delta(1-105)PttCel9A, TfCel9A, and TfCel9B were 0.023 +/- 0.001, 16.9 +/- 2.0, and 1.3 +/- 0.2, respectively. The catalytic efficiency (k(cat)/K-m) of TfCel9B was 39% of that of TfCel9A, whereas the catalytic efficiency of Delta(1-105)PttCel9A was 0.04% of that of TfCel9A. Removing tryptophan residues at subsites -4, -3, and -2 decreased the efficiency of cellohexaose hydrolysis by TfCel9A. Mutation of W313 to G had the most drastic effect, producing a mutant enzyme with 1% of the catalytic efficiency of TfCel9A. The apparent narrow substrate range and catalytic efficiency of PttCel9A are correlated with a lack of aromatic amino acids in the substrate binding cleft and may be necessary to prevent excessive hydrolysis of cell wall polysaccharides during cell wall formation.
650 7a TEKNIK OCH TEKNOLOGIERx Industriell bioteknik0 (SwePub)2092 hsv//swe
650 7a ENGINEERING AND TECHNOLOGYx Industrial Biotechnology0 (SwePub)2092 hsv//eng
653 a CULTURED POPLAR CELLS; IN-GEL DIGESTION; CELLULOSE SYNTHESIS; THERMOMONOSPORA-FUSCA; ARABIDOPSIS-THALIANA; AGROBACTERIUM-TUMEFACIENS; CRYSTAL-STRUCTURE; ENDO-1
653 a 4-BETA-GLUCANASE; PROTEINS; KORRIGAN
653 a Bioengineering
653 a Bioteknik
7001 a Rudsander, Ullau KTH,Bioteknologi4 aut0 (Swepub:kth)u1guywz3
7001 a Zhou, Welin4 aut
7001 a Henriksson, Hongbinu KTH,Bioteknologi4 aut0 (Swepub:kth)u1v3la4y
7001 a Divne, Christinau KTH,Bioteknologi,Industriell bioteknologi4 aut0 (Swepub:kth)u1mvd1wz
7001 a Denman, Stuartu KTH,Bioteknologi4 aut0 (Swepub:kth)u10abgkd
7001 a Wilson, David4 aut
7001 a Teeri, Tuulau KTH,Bioteknologi4 aut0 (Swepub:kth)u1vcejiv
7102 a KTHb Bioteknologi4 org
7730 t Biochemistryd : American Chemical Society (ACS)g 43:31, s. 10080-10089q 43:31<10080-10089x 0006-2960x 1520-4995
8564 u http://pubs.acs.org/cgi-bin/abstract.cgi/bichaw/2004/43/i31/abs/bi049453x.htmly Biochemistry
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-7587
8564 8u https://doi.org/10.1021/bi049453x

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