1992
DOI: 10.1111/j.1365-2958.1992.tb01379.x
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Homologous catalytic domains in a rumen fungal xylanase: evidence for gene duplication and prokaryotic origin

Abstract: A cDNA (xynA), encoding xylanase A (XYLA), was isolated from a cDNA library, derived from mRNA extracted from the rumen anaerobic fungus, Neocallimastix patriciarum. Recombinant XYLA, purified from Escherichia coli harbouring xynA, had a M(r) of 53,000 and hydrolysed oat-spelt xylan to xylobiose and xylose. The enzyme did not hydrolyse any cellulosic substrates. The nucleotide sequence of xynA revealed a single open reading frame of 1821 bp coding for a protein of M(r) 66,192. The predicted primary structure o… Show more

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Cited by 141 publications
(131 citation statements)
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“…AIR was prepared and analyzed by PACE, MS, and high-performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD) as described elsewhere (10,(40)(41)(42) and in SI Materials and Methods.…”
Section: Methodsmentioning
confidence: 99%
“…AIR was prepared and analyzed by PACE, MS, and high-performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD) as described elsewhere (10,(40)(41)(42) and in SI Materials and Methods.…”
Section: Methodsmentioning
confidence: 99%
“…The catalytic components of the Piromyces equi cellulosome do not contain CBMs (9,10), suggesting that the capacity of this enzyme complex to attach to the plant cell wall is mediated by one or a small number of noncatalytic proteins. Recently, the first of these noncatalytic components was identified.…”
mentioning
confidence: 99%
“…The plant cell wall degrading capacity of gut anaerobic fungi is vested in a multienzyme complex, termed the ''cellulosome'' (9), that binds to plant polysaccharides. The catalytic components of the Piromyces equi cellulosome do not contain CBMs (9,10), suggesting that the capacity of this enzyme complex to attach to the plant cell wall is mediated by one or a small number of noncatalytic proteins.…”
mentioning
confidence: 99%
“…The xynA and xyn11A possess two homologous catalytic domains and also two dockerin domains, whereas xyn11B has only one catalytic domain and two dockerin domains (Gilbert et al 1992;Huang et al 2005). In order to investigate the effects of dockerin domains on the enzyme activity, Huang et al (2005) deleted the dockerin domains from the xyn11A and xyn11B.…”
Section: Discussionmentioning
confidence: 99%
“…Xylanase genes of xynA (Gilbert et al 1992), xynB , xyn3 (Durand et al 1996), xynC (Liu et al 1999), xyn11A and xyn11B (Huang et al 2005) from Neocallimastix sp. were studied extensively.…”
Section: Introductionmentioning
confidence: 99%