KEGG ENZYME: 1.14.15.35

ENZYME: 1.14.15.35

Entry

EC 1.14.15.35               Enzyme

Name

6-deoxyerythronolide B hydroxylase;
DEB hydroxylase;
eryF (gene name);
P450(eryF);
CYP107A1

Class

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor

Sysname

6-deoxyerythronolide-B,reduced ferredoxin:oxygen oxidoreductase

Reaction(IUBMB)

6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O [RN:R05270]

Reaction(KEGG)

R05270

Substrate

6-deoxyerythronolide B [CPD:C03240];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
H+ [CPD:C00080];
O2 [CPD:C00007]

Product

erythronolide B [CPD:C06635];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
H2O [CPD:C00001]

Comment

A cytochrome P-450 (heme-thiolate) protein isolated from the bacterium Saccharopolyspora erythraea. The enzyme is involved in the biosynthesis of the antibiotic erythromycin.

History

EC 1.14.15.35 created 2014 as EC 1.14.13.188, transferred 2018 to EC 1.14.15.35

Pathway

ec00522

Biosynthesis of 12-, 14- and 16-membered macrolides

ec01100

Metabolic pathways

ec01110

Biosynthesis of secondary metabolites

Orthology

K14366

6-deoxyerythronolide B hydroxylase

Genes

SNR:	SNOUR_10185

SGF:	HEP81_07903

AER:	AERYTH_15880

SEN:	SACE_0730(eryF)

AEY:	CDG81_13145

Reference

1 [PMID:2011746]

Authors

Weber JM, Leung JO, Swanson SJ, Idler KB, McAlpine JB

Title

An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea.

Journal

Science 252:114-7 (1991)
DOI:10.1126/science.2011746

Sequence

[sen:SACE_0730]

Reference

2 [PMID:2446657]

Authors

Shafiee A, Hutchinson CR

Title

Macrolide antibiotic biosynthesis: isolation and properties of two forms of 6-deoxyerythronolide B hydroxylase from Saccharopolyspora erythraea (Streptomyces erythreus).

Journal

Biochemistry 26:6204-10 (1987)
DOI:10.1021/bi00393a037

Reference

3 [PMID:7846029]

Authors

Cupp-Vickery JR, Li H, Poulos TL

Title

Preliminary crystallographic analysis of an enzyme involved in erythromycin biosynthesis: cytochrome P450eryF.

Journal

Proteins 20:197-201 (1994)
DOI:10.1002/prot.340200210

Reference

4 [PMID:15824115]

Authors

Nagano S, Cupp-Vickery JR, Poulos TL

Title

Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF.

Journal

J Biol Chem 280:22102-7 (2005)
DOI:10.1074/jbc.M501732200

Sequence

[sen:SACE_0730]

Other DBs

ExplorEnz - The Enzyme Database:

1.14.15.35

IUBMB Enzyme Nomenclature:

1.14.15.35

ExPASy - ENZYME nomenclature database:

1.14.15.35

BRENDA, the Enzyme Database:

1.14.15.35

DBGET integrated database retrieval system