Crystal Structure of Maltose Phosphorylase from Lactobacillus brevis

Egloff, Marie‐Pierre; Uppenberg, J.; Haalck, Lutz; Tilbeurgh, Herman van

doi:10.1016/s0969-2126(01)00626-8

Cited by 121 publications

(92 citation statements)

References 39 publications

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“…This basic fold is common in glycosyl hydrolases, polysaccharide lyases, and terpenoid cylases/protein prenyltransferases in the SCOP data base (scop.mrc-lmb.cam.ac.uk/scop/ data/scop.b.b.bcj.html) (34). UGL has the ␣ 6 /␣ 6 -barrel found in the six-hairpin enzyme superfamily of the SCOP data base, which includes glucoamylases (35-37), cellulase catalytic domains (38 -40), N-acyl-D-glucosamine 2-epimerase (AGE) (41), the maltose phosphorylase central domain (42), and hypothetical protein Yter. Based on the structural similarity in the RCSB Protein Data Bank (28) observed with the DALI (29) program, three proteins, i.e.…”

Section: Resultsmentioning

confidence: 99%

Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 Å Resolution

Itoh

Akao

Hashimoto

et al. 2004

Journal of Biological Chemistry

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Unsaturated glucuronyl hydrolase (UGL) is a novel glycosaminoglycan hydrolase that releases unsaturated D-glucuronic acid from oligosaccharides produced by polysaccharide lyases. The x-ray crystallographic structure of UGL from Bacillus sp. GL1 was first determined by multiple isomorphous replacement (mir) and refined at 1.8 Å resolution with a final R-factor of 16.8% for 25 to 1.8 Å resolution data. The refined UGL structure consists of 377 amino acid residues and 478 water molecules, four glycine molecules, two dithiothreitol (DTT) molecules, and one 2-methyl-2,4-pentanediol (MPD) molecule. UGL includes an ␣ 6 /␣ 6 -barrel, whose structure is found in the six-hairpin enzyme superfamily of an ␣/␣-toroidal fold. One side of the UGL ␣ 6 /␣ 6 -barrel structure consists of long loops containing three short ␤-sheets and contributes to the formation of a deep pocket. One glycine molecule and two DTT molecules surrounded by highly conserved amino acid residues in UGLs were found in the pocket, suggesting that catalytic and substrate-binding sites are located in this pocket. The overall UGL structure, with the exception of some loops, very much resembled that of the Bacillus subtilis hypothetical protein Yter, whose function is unknown and which exhibits little amino acid sequence identity with UGL. In the active pocket, residues possibly involved in substrate recognition and catalysis by UGL are conserved in UGLs and Yter. The most likely candidate catalytic residues for glycosyl hydrolysis are Asp 88 and Asp 149 . This was supported by site-directed mutagenesis studies in Asp 88 and Asp 149 .

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Section: Resultsmentioning

confidence: 99%

Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 Å Resolution

Itoh

Akao

Hashimoto

et al. 2004

Journal of Biological Chemistry

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“…All of these GH enzymes contain the (α/α) 6 barrel or a similar domain in their structures. This paper describes enzymes of the families GH65, GH78, GH92, GH94, and GH95, the catalytic domains of enzymes of these families show high homology with those of GH15, GH37, and GH63 (Table I) Although the GH65 contains some acid trehalases (38), numerous phosphorylases are classified into GH65 (e.g., maltose phosphorylase and trehalose phosphorylase) (39,40) and GH94 (e.g., chitobiose phosphorylase and cellobiose phosphorylase) (41,42). Lactobacillus brevis maltose phosphorylase (GH65; Fig.…”

Section: Enzymes Structurally Related To Enzymes Of the Families Gmentioning

confidence: 99%

“…Lactobacillus brevis maltose phosphorylase (GH65; Fig. 3A) (39) and Vibrio proteolyticus chitobiose phosphorylase (GH94; Fig. 3B) (41) are composed of an N-terminal super β-sandwich domain and a C-terminal catalytic (α/α) 6 barrel domain, and their architectures are similar to those of T. thermosaccharolyticum glucoamylase (GH15) and E. coli YgjK (GH63).…”

Section: Enzymes Structurally Related To Enzymes Of the Families Gmentioning

confidence: 99%

“…The catalytic mechanism of the GH65 and GH94 phosphorylases is identical to that of the GH15, GH37, and GH63 hydrolases. The general acid catalyst corresponding to Glu179 in A. awamori glucoamylase is identified as Glu487 in L. brevis GH65 maltose phosphorylase (39) and Asp492 in V. proteolyticus GH94 chitobiose phosphorylase (41). The residue that acts as a general base, corresponding to Glu400 in A. awamori glucoamylase, is substituted for a phosphate ion in both GH65 and GH94 (11).…”

Section: Enzymes Structurally Related To Enzymes Of the Families Gmentioning

confidence: 99%

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Structural Similarity between a Starch-hydrolyzing Enzyme and an N-Glycan-Hydrolyzing Enzyme: Exohydrolases Cleaving α-1,X-Glucosidic Linkages to Produce β-Glucose

Tonozuka

Miyazaki

Nishikawa

2011

TIGG

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Glucoamylase, glucodextranase, trehalase, and eukaryotic N-glycan processing α-glucosidase I have been identified as exo-acting enzymes that hydrolyze α-1,Xglucosidic linkages from the non-reducing end to produce β-glucose. While the physiological functions of these enzymes are different, they share a catalytic (α/α) 6 barrel domain and show many structural similarities. These enzymes, with few exceptions, belong to the glycoside hydrolase families (GHs) 15, 37, and 63 in the CAZy database, and all these enzymes have 2 conserved aspartic or glutamic acid residues in the catalytic domain. The observations led us to consider that the group of GH15, GH37, and GH63 may be designated as a "glucoamylase family." There are also many hydrolases and phosphorylases structurally related to GH15, GH37, and GH63.

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“…GL1, 56,57) a plant cell wall-degrading enzyme (B. subtilis unsaturated galacturonyl hydrolase) YteR, 58) and an AGE structural homolog, YihS, (unpublished) of S. typhimurium have = -barrel structures as a basic scaffold. The = -barrel structure is also found in sugarrelated enzymes such as glucoamylase, 59) endoglucanases, 60) endo/exo-cellulase, 61) -1,2-mannosidase, 62) and maltose phosphorylase, 63) as well as polysaccharide lyases. These enzymes form the = -toroid family in the SCOP database (http://scop.berkeley.edu/data/scop.b.b.…”

Section: Structural Features Of Polysaccharide Lyasementioning

confidence: 99%