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Your query returned 4 entries. Printable version

2.4.1.338

Accepted name:

validoxylamine A glucosyltransferase

Reaction:

UDP-α-D-glucose + validoxylamine A = UDP + validamycin A

For diagram of validamycin biosynthesis, click here

Glossary:

validoxylamine A = (1S,2S,3R,6S)-4-(hydroxymethyl)-6-{[(1S,2S,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}cyclohex-4-ene-1,2,3-triol

Other name(s):

vldK (gene name); valG (gene name)

Systematic name:

UDP-α-D-glucose:validoxylamine-A 4′-O-glucosyltransferase

Comments:

The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, catalyses the ultimate step in the biosynthesis of the antifungal agent validamycin A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Bai, L., Li, L., Xu, H., Minagawa, K., Yu, Y., Zhang, Y., Zhou, X., Floss, H.G., Mahmud, T. and Deng, Z. Functional analysis of the validamycin biosynthetic gene cluster and engineered production of validoxylamine A. Chem. Biol. 13 (2006) 387–397. [DOI] [PMID: 16632251]
2.	Xu, H., Minagawa, K., Bai, L., Deng, Z. and Mahmud, T. Catalytic analysis of the validamycin glycosyltransferase (ValG) and enzymatic production of 4′′-epi-validamycin A. J Nat Prod 71 (2008) 1233–1236. [DOI] [PMID: 18563934]

[EC 2.4.1.338 created 2016]

2.5.1.135

Accepted name:

validamine 7-phosphate valienyltransferase

Reaction:

GDP-valienol + validamine 7-phosphate = validoxylamine A 7′-phosphate + GDP

For diagram of validamycin biosynthesis, click here

Glossary:

valienol = (1S,2S,3S,4R)-5-(hydroxymethyl)cyclohex-5-ene-1,2,3,4-tetrol
validamine = (1R,2S,3S,4S,6R)-4-amino-6-(hydroxymethyl)cyclohexane-1,2,3-triol

Other name(s):

vldE (gene name); valL (gene name)

Systematic name:

GDP-valienol:validamine 7-phosphate valienyltransferase

Comments:

The enzyme, characterized from several Streptomyces strains, is involved in the biosynthesis of the antifungal agent validamycin A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Asamizu, S., Yang, J., Almabruk, K.H. and Mahmud, T. Pseudoglycosyltransferase catalyzes nonglycosidic C-N coupling in validamycin a biosynthesis. J. Am. Chem. Soc. 133 (2011) 12124–12135. [DOI] [PMID: 21766819]
2.	Zheng, L., Zhou, X., Zhang, H., Ji, X., Li, L., Huang, L., Bai, L. and Zhang, H. Structural and functional analysis of validoxylamine A 7′-phosphate synthase ValL involved in validamycin A biosynthesis. PLoS One 7:e32033 (2012). [DOI] [PMID: 22384130]
3.	Cavalier, M.C., Yim, Y.S., Asamizu, S., Neau, D., Almabruk, K.H., Mahmud, T. and Lee, Y.H. Mechanistic insights into validoxylamine A 7′-phosphate synthesis by VldE using the structure of the entire product complex. PLoS One 7:e44934 (2012). [DOI] [PMID: 23028689]

[EC 2.5.1.135 created 2016]

3.1.3.101

Accepted name:

validoxylamine A 7′-phosphate phosphatase

Reaction:

validoxylamine A 7′-phosphate + H₂O = validoxylamine A + phosphate

For diagram of validamycin biosynthesis, click here

Glossary:

validoxylamine A = (1S,2S,3R,6S)-4-(hydroxymethyl)-6-{[(1S,2S,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}cyclohex-4-ene-1,2,3-triol

Other name(s):

vldH (gene name)

Systematic name:

validoxylamine-A 7′-phosphate phosphohydrolase

Comments:

The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, is involved in the biosynthesis of the antifungal agent validamycin A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Asamizu, S., Yang, J., Almabruk, K.H. and Mahmud, T. Pseudoglycosyltransferase catalyzes nonglycosidic C-N coupling in validamycin a biosynthesis. J. Am. Chem. Soc. 133 (2011) 12124–12135. [DOI] [PMID: 21766819]

[EC 3.1.3.101 created 2016]

4.3.3.1

Accepted name:

3-ketovalidoxylamine C-N-lyase

Reaction:

4-nitrophenyl-3-ketovalidamine = 4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one

Other name(s):

3-ketovalidoxylamine A C-N-lyase; p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase; 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase

Systematic name:

4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase [5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one-forming]

Comments:

Requires Ca²⁺. Eliminates 4-nitroaniline from 4-nitrophenyl-3-ketovalidamine, or 4-nitrophenol from 4-nitrophenyl-α-D-3-dehydroglucoside. Involved in the degradation of the fungicide validamycin A by Flavobacterium saccharophilum.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99889-98-2

References:

1.	Asano, N., Takeuchi, M., Ninomiya, K., Kameda, Y. and Matsui, K. Microbial degradation of validamycin A by Flavobacterium saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A. J. Antibiot. 37 (1984) 859–867. [PMID: 6548220]
2.	Takeuchi, M., Asano, N., Kameda, Y. and Matsui, K. Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum. J. Biochem. (Tokyo) 98 (1985) 1631–1638. [PMID: 4093450]

[EC 4.3.3.1 created 1989]