Gene_locus Report for: 9bace-b3cet1

Bacteroides intestinalis DSM 17393 Bacint_04212 BiFae1A ferulic acid esterase

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > FCB group: N E > Bacteroidetes/Chlorobi group: N E > Bacteroidetes: N E > Bacteroidia: N E > Bacteroidales: N E > Bacteroidaceae: N E > Bacteroides: N E > Bacteroides intestinalis: N E > Bacteroides intestinalis DSM 17393: N E

A85-EsteraseD-FGH : 9bace-b3che1Bacteroides intestinalis DSM 17393 Putative uncharacterized protein.
A85-Feruloyl-Esterase : 9bace-b3c9d0.2Bacteroides intestinalis DSM 17393 BiFae1B Putative uncharacterized protein, 9bace-b3c594Bacteroides intestinalis DSM 17393 Putative uncharacterized protein, 9bace-b3c969 Bacteroides intestinalis DSM 17393 feruloyl esterase, Bacint_01033 isoamylase N-terminal domain protein, 9bace-b3c974Bacteroides intestinalis DSM 17393 Putative uncharacterized protein BACINT_01038-CE6/CE1, 9bace-b3c975 Bacteroides intestinalis DSM 17393 BACINT_01039-CE1 Putative uncharacterized protein.
A85-IroE-IroD-Fes-Yiel : 9bace-b3cb92Bacteroides intestinalis DSM 17393 Putative uncharacterized protein, 9bace-b3ci38Bacteroides intestinalis DSM 17393 Putative uncharacterized protein.
Abhydrolase_7 : 9bace-b3cg27Bacteroides intestinalis Putative uncharacterized protein, 9bace-b3cg28Bacteroides intestinalis, Putative uncharacterized protein.
Acetyl-esterase_deacetylase : 9bace-b3c7p2Bacteroides intestinalis DSM 17393 Acetyl xylan esterase (AXE1), 9bace-b3cg29Bacteroides intestinalis DSM 17393 Acetyl xylan esterase (AXE1).
Bacterial_EstLip_FamX : 9bace-b3cfy2Bacteroides intestinalis DSM 17393 Putative uncharacterized protein.
BD-FAE : 9bace-b3c976Bacteroides intestinalis esterase BACINT_01040, 9bace-b3caa7Bacteroides intestinalis DSM 17393 Putative uncharacterized protein.
BioG_Pimeloyl-ACP-methyl-esterase : 9bace-b3cav2Bacteroides intestinalis DSM 17393 Putative uncharacterized protein.
DPP4N_Peptidase_S9 : 9bace-b3c6j1Bacteroides intestinalis, Bacteroides cellulosilyticus, Putative uncharacterized protein, 9bace-b3c948Bacteroides intestinalis DSM 17393 Putative uncharacterized protein, 9bace-b3cg11Bacteroides intestinalis, Bacteroides cellulosilyticus, Putative uncharacterized protein.
Peptidase_S37 : 9bace-b3c8j8Bacteroides intestinalis DSM 17393 Putative uncharacterized protein.
PolyAspartate-hydrolase : 9bace-b3c5f6Bacteroides intestinalis DSM 17393 Bacteroides cellulosilyticus DSM 14838 Putative uncharacterized protein

Title: Biochemical and Structural Analyses of Two Cryptic Esterases in Bacteroides intestinalis and their Synergistic Activities with Cognate Xylanases
Wefers D, Cavalcante JJV, Schendel RR, Deveryshetty J, Wang K, Wawrzak Z, Mackie RI, Koropatkin NM, Cann I
Ref: Journal of Molecular Biology, 429:2509, 2017 : PubMed
Abstract


ESTHER: Wefers_2017_J.Mol.Biol_429_2509
PubMedSearch: Wefers 2017 J.Mol.Biol 429 2509
PubMedID: 28669823
Gene_locus related to this paper: 9bace-b3c9d0.2, 9bace-b3cet1

Abstract

Arabinoxylans are constituents of the human diet. Although not utilizable by the human host, they can be fermented by colonic bacteria. The arabinoxylan backbone is decorated with arabinose side chains that may be substituted with ferulic acid, thus limiting depolymerization to fermentable sugars. We investigated the polypeptides encoded by two genes upregulated during growth of the colonic bacterium Bacteroides intestinalis on wheat arabinoxylan. The recombinant proteins, designated BiFae1A and BiFae1B, were functionally assigned esterase activities. Both enzymes were active on acetylated substrates, although each showed a higher ferulic acid esterase activity on methyl-ferulate. BiFae1A showed a catalytic efficiency of 12mM s(-1) on para-nitrophenyl-acetate, and on methyl-ferulate, the value was 27 times higher. BiFae1B showed low catalytic efficiencies for both substrates. Furthermore, the two enzymes released ferulic acid from various structural elements, and NMR spectroscopy indicated complete de-esterification of arabinoxylan oligosaccharides from wheat bran. BiFae1A is a tetramer based on the crystal structure, whereas BiFae1B is a dimer in solution based on size exclusion chromatography. The structure of BiFae1A was solved to 1.98A resolution, and two tetramers were observed in the asymmetric unit. A flexible loop that may act as a hinge over the active site and likely coordinates critical interactions with the substrate was prominent in BiFae1A. Sequence alignments of the esterase domains in BiFae1B with the feruloyl esterase from Clostridium thermocellum suggest that both domains lack the flexible hinge in BiFae1A, an observation that may partly provide a molecular basis for the differences in activities in the two esterases.