Literature summary for 3.2.1.96 extracted from

Ling, Z.; Suits, M.D.; Bingham, R.J.; Bruce, N.C.; Davies, G.J.; Fairbanks, A.J.; Moir, J.W.; Taylor, E.J.
The X-ray crystal structure of an Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase reveals a (beta/alpha)8 catalytic domain, two ancillary domains and active site residues key for transglycosylation activity (2009), J. Mol. Biol., 389, 1-9.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), and of selenomethionine-labeled enzymes in strain B834(DE3)	Glutamicibacter protophormiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
purifed recombinant wild-type enzyme and mutant E173Q in unlabeled or selenomethionine-labeled forms, 1:1 mixture of 42 mg/mL protein with a reservoir solution consisting of 0.35 M KSCN, 0.1 M 1,3-bis(tris(hydroxymethyl)methylamino)propane, pH 6.5, and 15% w/v PEG 3350, 30 days at 4 °C for the unlabeled, and 14 days at 18 °C for the SeM-labeled enzymes, X-ray diffraction and analysis at 1.8 A resolution, multiple-wavelength anomalous scattering methods, structure modelling, overview	Glutamicibacter protophormiae

Crystallization (Comment)

Organism

purifed recombinant wild-type enzyme and mutant E173Q in unlabeled or selenomethionine-labeled forms, 1:1 mixture of 42 mg/mL protein with a reservoir solution consisting of 0.35 M KSCN, 0.1 M 1,3-bis(tris(hydroxymethyl)methylamino)propane, pH 6.5, and 15% w/v PEG 3350, 30 days at 4 °C for the unlabeled, and 14 days at 18 °C for the SeM-labeled enzymes, X-ray diffraction and analysis at 1.8 A resolution, multiple-wavelength anomalous scattering methods, structure modelling, overview

Glutamicibacter protophormiae

Protein Variants

Protein Variants	Comment	Organism
E173Q	site-directed mutagenesis, the mutant shows increased transglycosylation activity compared to the wild-type enzyme, three-dimensional structure determination and analysis, overview	Glutamicibacter protophormiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Glutamicibacter protophormiae	the enzyme is responsible for the hydrolysis of beta-1,4 linkage in the N,Ndiacetylchitobiose core of N-linked glycans. It also shows transglycosylation activity	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Glutamicibacter protophormiae	Q9ZB22	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
(Man)3(GlcNAc)2Asn + H2O = (Man)3GlcNAc + GlcNAc-Asn	active site structure, catalytic mechanism in which residue E173 acts as the catalytic acid/base for reaction via an oxazoline intermediate, overview	Glutamicibacter protophormiae	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme is responsible for the hydrolysis of beta-1,4 linkage in the N,Ndiacetylchitobiose core of N-linked glycans. It also shows transglycosylation activity	Glutamicibacter protophormiae	?	-	?
additional information	active site structure, catalytic mechanism in which residue E173 acts as the catalytic acid/base for reaction via an oxazoline intermediate, asparagine in the active centre is in a position likely to interact with the acetyl NH group. Three-dimensional structure of this important biocatalyst reveals that residues implicated in the enhancement of transglycosylation and synthetic capacity are proximal to the active centre, where they may act to favor binding of acceptor substrates	Glutamicibacter protophormiae	?	-	?

Subunits

Subunits	Comment	Organism
More	the GH85 enzyme Endo-A displays a trimodular architecture in which a (betaalpha)8 catalytic domain occurs with two ancillary beta-sheet modules	Glutamicibacter protophormiae

Synonyms

Synonyms	Comment	Organism
Endo-A	-	Glutamicibacter protophormiae
endo-beta-N-acetylglucosaminidase	-	Glutamicibacter protophormiae
More	the enzyme belongs to the glycoside hydrolase family 85, GH85	Glutamicibacter protophormiae