4.3.3.1	648712	Chemical modification by 2,4,6-trinitrobenzenesulfonic acid (TNBS) of an essential amino group in 3-ketovalidoxylamine A C-N lyase	Chem. Pharm. Bull.	38	1419-1420	1990	Flavobacterium saccharophilum	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=2393971&form=6&db=m	
4.3.3.1	648710	Chemical modification by diethylpyrocarbonate of an essential histidine residue in 3-ketovalidoxylamine A C-N lyase	J. Biochem.	99	1571-1577	1986	Flavobacterium saccharophilum	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3745136&form=6&db=m	
4.3.3.1	648711	Fluorometric studies on the role of calcium in substrate binding to 3-ketovalidoxylamine A C-N lyase	Chem. Pharm. Bull.	36	3540-3545	1988	Flavobacterium saccharophilum	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3240546&form=6&db=m	
4.3.3.1	714560	Gene cloning and expression of a 3-ketovalidoxylamine C-N-lyase from Flavobacterium saccharophilum IFO 13984	Biotechnol. Bioprocess Eng.	16	366-373	2011	Flavobacterium saccharophilum	-	
4.3.3.1	714560	Gene cloning and expression of a 3-ketovalidoxylamine C-N-lyase from Flavobacterium saccharophilum IFO 13984	Biotechnol. Bioprocess Eng.	16	366-373	2011	Flavobacterium saccharophilum IFO 13984	-	
4.3.3.1	648708	Microbial degradation of validamycin A by Flavobacterium saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A	J. Antibiot.	37	859-867	1984	Flavobacterium saccharophilum	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6548220&form=6&db=m	
4.3.3.1	677731	Preparation of 3-ketovalidoxylamine A C-N lyase substrate: N-p-nitrophenyl-3-ketovalidamine by Stenotrophomonas maltrophilia CCTCC M 204024	Appl. Microbiol. Biotechnol.	73	1275-1281	2007	Stenotrophomonas maltophilia	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=17058074&form=6&db=m	
4.3.3.1	701773	Purification and Characterization of 3-Ketovalidoxylamine A C-N Lyase Produced by Stenotrophomonas maltrophilia	Appl. Biochem. Biotechnol.	162	966-74	2010	Stenotrophomonas maltophilia	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19795222&form=6&db=m	
4.3.3.1	648709	Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum	J. Biochem.	98	1631-1638	1985	Flavobacterium saccharophilum	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=4093450&form=6&db=m	
4.3.3.1	701595	Study on optimal production of 3-ketovalidoxylamine A C-N lyase and glucoside 3-dehydrogenase by a newly isolated Stenotrophomonas maltrophilia	Afr. J. Biotechnol.	8	5482-5488	2009	Stenotrophomonas maltophilia	-