Literature summary extracted from

Giastas, P.; Andreou, A.; Papakyriakou, A.; Koutsioulis, D.; Balomenou, S.; Tzartos, S.J.; Bouriotis, V.; Eliopoulos, E.E.
Structures of the peptidoglycan N-acetylglucosamine deacetylase Bc1974 and its complexes with zinc metalloenzyme inhibitors (2018), Biochemistry, 57, 753-763 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
3.5.1.104	gene BC_1974, sequence comaprisons	Bacillus cereus

EC Number	Crystallization (Comment)	Organism
3.5.1.104	crystal structure analysis of Zn-bound and acetate-bound Bc1974 enzyme, PDB ID 5N1J, structure comparisons. Analysis of X-ray crystal structures of the NodB domain of Bc1974, the conserved catalytic core of CE4s, in the unliganded form and in complex with four known metalloenzyme inhibitors and two amino acid hydroxamates that target the active site metal	Bacillus cereus

EC Number	Inhibitors	Comment	Organism
3.5.1.104	1-naphthohydroxamic acid	complete inhibition at 0.5 mM	Bacillus cereus
3.5.1.104	3-biphenyl-hydroxamic acid	-	Bacillus cereus
3.5.1.104	acetazolamide	-	Bacillus cereus
3.5.1.104	actinonin	-	Bacillus cereus
3.5.1.104	batimastat	-	Bacillus cereus
3.5.1.104	CP-471474	-	Bacillus cereus
3.5.1.104	DL-methionine	-	Bacillus cereus
3.5.1.104	DL-phenylalanine	-	Bacillus cereus
3.5.1.104	DL-Serine hydroxamate	-	Bacillus cereus
3.5.1.104	L-Arginine hydroxamate	-	Bacillus cereus
3.5.1.104	L-Lysine hydroxamate	-	Bacillus cereus
3.5.1.104	marimastat	-	Bacillus cereus
3.5.1.104	N'-hydroxy-N-(2-methyl-5-nitrophenyl)oxamide	-	Bacillus cereus
3.5.1.104	N-hydroxy-(4-naphthalen-1-yl)benzazmide	-	Bacillus cereus
3.5.1.104	N-hydroxy-2,2-diphenylacetamide	-	Bacillus cereus
3.5.1.104	N-hydroxy-3-(naphthalen-1-yl)acrylamide	-	Bacillus cereus
3.5.1.104	N-hydroxy-3-phenoxybenzamide	-	Bacillus cereus
3.5.1.104	N-hydroxy-4-(isoquinolin-4-yl)benzamide	-	Bacillus cereus
3.5.1.104	N5-hydroxy-L-glutamine	-	Bacillus cereus
3.5.1.104	streptozotocin	-	Bacillus cereus
3.5.1.104	thiamet G	-	Bacillus cereus
3.5.1.104	UK-356618	-	Bacillus cereus
3.5.1.104	verinostat	i.e. SAHA	Bacillus cereus
3.5.1.104	Z-Pro-Leu-Gly hydroxamate	-	Bacillus cereus
3.5.1.104	Z-PUGNAc	-	Bacillus cereus

EC Number	Metals/Ions	Comment	Organism	Structure
3.5.1.104	Zn2+	a zinc metalloenzyme, active site metal	Bacillus cereus

EC Number	Organism	UniProt	Comment	Textmining
3.5.1.104	Bacillus cereus	Q81EJ6	-	-
3.5.1.104	Bacillus cereus ATCC 14579	Q81EJ6	-	-
3.5.1.104	Bacillus cereus DSM 31	Q81EJ6	-	-
3.5.1.104	Bacillus cereus JCM 2152	Q81EJ6	-	-
3.5.1.104	Bacillus cereus NBRC 15305	Q81EJ6	-	-
3.5.1.104	Bacillus cereus NCIMB 9373	Q81EJ6	-	-
3.5.1.104	Bacillus cereus NRRL B-3711	Q81EJ6	-	-

EC Number	Synonyms	Comment	Organism
3.5.1.104	Bc1974	-	Bacillus cereus
3.5.1.104	peptidoglycan N-acetylglucosamine deacetylase	-	Bacillus cereus

EC Number	General Information	Comment	Organism
3.5.1.104	evolution	Bacillus cereus, a close relative of the highly virulent Bacillus anthracis, contains 10 polysaccharide deacetylases. Among these, the peptidoglycan N-acetylglucosamine deacetylase Bc1974 is the highest homologue to the Bacillus anthracis Ba1977 that is required for full virulence and is involved in resistance to the host's lysozyme. These metalloenzymes belong to the carbohydrate esterase family 4 (CE4)	Bacillus cereus
3.5.1.104	additional information	Bc1974 substrate docking and molecular modelling, overview. Presence of two conformational states of a catalytic loop known as motif-4 (MT4) previously unknown for peptidoglycan deacetylases, comparison to structure of a Vibrio clolerae chitin deacetylase. The deduced catalytic mechanism probably involves initial binding of the substrate in a receptive, more open state of MT4 and optimal catalytic activity in the closed state of MT4	Bacillus cereus