4.3.3.1: 3-ketovalidoxylamine C-N-lyase

This is an abbreviated version!
For detailed information about 3-ketovalidoxylamine C-N-lyase, go to the full flat file.

Word Map on EC 4.3.3.1

4.3.3.1

saccharophilum

flavobacterium

stenotrophomonas

pseudo-first

ethylenediaminetetraacetic

half-time

medicine

Reaction

5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one

Synonyms

3-ketovalidoxylamine A C-N lyase, 3-ketovalidoxylamine A C-N-lyase, 3-ketovalidoxylamine C-N-lyase, lyase, 3-ketovalidoxylamine A C-N-, p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase

ECTree

4 Lyases

4.3 Carbon-nitrogen lyases

4.3.3 Amine-lyases

4.3.3.1 3-ketovalidoxylamine C-N-lyase

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Results	in table
1	Application
1	CAS Registry Number
1	Cloned(Commentary)
1	General Stability
15	Inhibitors
2	Ki Value [mM]
5	KM Value [mM]
3	Localization
5	Metals/Ions
7	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
10	Organism
4	pH Optimum
1	pH Range
1	pH Stability
1	pI Value
2	Posttranslational Modification
2	Purification (Commentary)
1	Reaction
4	Reaction Type
10	Reference
3	Specific Activity [micromol/min/mg]
1	Storage Stability
25	Substrates and Products (Substrate)
3	Subunits
7	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Stability [°C]

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Reference on EC 4.3.3.1 - 3-ketovalidoxylamine C-N-lyase

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648708

Asano, N.; Takeuchi, M.; Ninomiya, K.;Kameda, Y.; Matsui, K.

Microbial degradation of validamycin A by Flavobacterium saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A

J. Antibiot.

859-867

1984

Flavobacterium saccharophilum

6548220

648709

Takeuchi, M.; Asano, N.; Kameda, Y.; Matsui, K.

Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum

J. Biochem.

1631-1638

1985

Flavobacterium saccharophilum

4093450

648710

Takeuchi, M.; Asano, N.; Kameda, Y.; Matsui, K.

Chemical modification by diethylpyrocarbonate of an essential histidine residue in 3-ketovalidoxylamine A C-N lyase

J. Biochem.

1571-1577

1986

Flavobacterium saccharophilum

3745136

648711

Takeuchi, M.; Asano, N.; Kameda, Y.; Matsui, K.

Fluorometric studies on the role of calcium in substrate binding to 3-ketovalidoxylamine A C-N lyase

Chem. Pharm. Bull.

3540-3545

1988

Flavobacterium saccharophilum

3240546

648712

Takeuchi, M.; Neyazaki, K.; Matsui, K.

Chemical modification by 2,4,6-trinitrobenzenesulfonic acid (TNBS) of an essential amino group in 3-ketovalidoxylamine A C-N lyase

Chem. Pharm. Bull.

1419-1420

1990

Flavobacterium saccharophilum

2393971

677731

Zhang, J.F.; Zheng, Y.G.; Liu, Z.Q.; Shen, Y.C.

Preparation of 3-ketovalidoxylamine A C-N lyase substrate: N-p-nitrophenyl-3-ketovalidamine by Stenotrophomonas maltrophilia CCTCC M 204024

Appl. Microbiol. Biotechnol.

1275-1281

2007

Stenotrophomonas maltophilia

17058074

701595

Zhang, J.; Zheng, Y.; Shen, Y.

Study on optimal production of 3-ketovalidoxylamine A C-N lyase and glucoside 3-dehydrogenase by a newly isolated Stenotrophomonas maltrophilia

Afr. J. Biotechnol.

5482-5488

2009

Stenotrophomonas maltophilia

701773

Zhang, J.F.; Zheng, Y.G.; Shen, Y.C.

Purification and Characterization of 3-Ketovalidoxylamine A C-N Lyase Produced by Stenotrophomonas maltrophilia

Appl. Biochem. Biotechnol.

162

966-74

2010

Stenotrophomonas maltophilia

19795222

714560

Kim, J.; Joo, J.; Kim, S.; Yoo, Y.

Gene cloning and expression of a 3-ketovalidoxylamine C-N-lyase from Flavobacterium saccharophilum IFO 13984

Biotechnol. Bioprocess Eng.

366-373

2011

Flavobacterium saccharophilum (DI109203), Flavobacterium saccharophilum IFO 13984 (DI109203)