Biochemical and Biophysical Research Communications
Purification and analysis of the structure of α-galactosidase from
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Cited by (30)
Structure of an α-glucuronidase in complex with Co<sup>2+</sup> and citrate provides insights into the mechanism and substrate recognition in the family 4 glycosyl hydrolases
2019, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Notably, the GH4 requires a divalent metal ion and reducing conditions for activity. This family includes six groups of enzymes with different specificities: α-glucosidase [6], α-galactosidase [7], α-galacturonidase [8], α-glucuronidase [9], phospho-α-glucosidase [4] and phospho-β-glucosidase [5], while some of them show activity on both α- and β-glycosidic linkages [4]. Crystal structures of only eight GH4 homologs are available in the PDB and those representing four of the specificities have been reported in literature [4–6,8], while the others are results from structural genomics projects.
A protease-resistant α-galactosidase from Pleurotus citrinopileatus with broad substrate specificity and good hydrolytic activity on raffinose family oligosaccharides
2016, Process BiochemistryCitation Excerpt :Thus, PCGI is a heterodimer in solution. It has been reported that T. polysaccharolyticum [28] and T. maritima Gal A [29], and Escherichia coli Mel A [30] were active as dimers. High-quality MALDI-TOF peptide mass spectrum was obtained after tryptic digestion of PCGI.
α-Galacturonidase(s): A new class of Family 4 glycoside hydrolases with strict specificity and a unique CHEV active site motif
2013, FEBS LettersCitation Excerpt :Significantly, and in contrast with Koshland’s double-displacement mechanisms [8–11], members of GH4 catalyze the hydrolysis of the glycosidic linkage via a novel sequence of oxidation–elimination–addition and reduction reactions [11–17]. The GH4 Family is also unique in that it includes five groups of enzymes [18], whose substrate specificities correlate remarkably with the presence of a four amino acid motif including the active-site Cysteine residue: 6-phospho-β-glucosidases, CN(V/I)P [5,9,11,13], 6-phospho-α-glucosidases, CDMP [4,12,19,20], α-glucosidases, CHEI [6,7,21], α-galactosidases, CH(S/G)V [3,22–24] and α-glucuronidases, CHGx [25]. In an earlier phylogenetic analysis of 201 GH4 enzymes, we noted a group of proteins of unknown catalytic activity with the motif CHEV (see Fig. 1A, Ref. [18]).
Genes malh and pagl of Clostridium acetobutylicum ATCC 824 Encode NAD <sup>+</sup>- and Mn<sup>2+</sup>-dependent Phospho-α-glucosidase(s)
2004, Journal of Biological ChemistryCitation Excerpt :The mass difference was attributed to an additional Gly residue and an oxidation. Cofactor Requirements and Substrate Specificity of PagL and MalH—Previous studies of proteins assigned to GHF4 (14, 16, 17, 20-22), have shown that NAD+, Mn2+ ion, and DTT are prerequisites for enzyme activity. Data presented in Table I show that both MalH and PagL are dependent upon these same cofactors for hydrolysis of the chromogenic substrate, pNPαGlc6P.
The Aes protein and the monomeric α-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism
2002, Journal of Biological ChemistryCitation Excerpt :These results could indicate specificity in the Aes/α-galactosidase interaction and non-specificity in the formation of Aes dimers (see below). It has been reported that the E. coli α-galactosidase is active in its tetrameric form and it requires magnesium ions and NAD for activity (32). We observed that NADH can substitute NAD in this role (no activity was observed in the absence of NADH).
β-glucoside kinase (BglK) from Klebsiella pneumoniae. Purification, properties, and preparative synthesis of 6-phospho-β-D-glucosides
2002, Journal of Biological ChemistryCitation Excerpt :The four disaccharide-6′-Ps and related P-β-glucoside analogs are substrates for Family 4 P-β-glucosylhydrolases. This large family of NAD+- and Me2+-dependent bacterial enzymes includes P-β-glucosidases, P-α-glucosidases, and α-glycosylhydrolases (11-16).2 A preliminary x-ray analysis of one P-α-glucosidase (GlvA) from Bacillus subtilis has been reported (10), but the complete structure of a Family 4 member has yet to be solved. The availability of the P-β-glucosides described here will assist in the crystallization, structural analysis, and elucidation of the catalytic mechanism (inversion or retention (35-37)) of Family 4 enzymes.