BRENDA - Reference to 1.13.11.72; Id = 719645

Acetylphosphate

-

Streptomyces viridochromogenes

Q5IW40

-

(2R)-hydroxypropylphosphonate + O2

-

719645

Streptomyces viridochromogenes

2-oxopropylphosphonate + hydroxymethylphosphonate + acetate

substrate partitions between conversion to 2-oxopropylphosphonate and hydroxymethylphosphonate

-

?

1-hydroxy-2,2,2-trifluoroethylphosphonate + O2

-

719645

Streptomyces viridochromogenes

trifluoroacetylphosphonate

-

?

1-hydroxyethylphosphonate + O2

-

719645

Streptomyces viridochromogenes

acetylphosphate

-

?

2-hydroxyethylphosphonate + O2

-

719645

Streptomyces viridochromogenes

hydroxymethylphosphonate + formate

-

?

hydroxymethylphosphonate + O2

-

719645

Streptomyces viridochromogenes

phosphate + formate

-

?

additional information

results provide strong support for a mechanism that proceeds by hydroperoxylation followed by a Criegee rearrangement with a phosphorus-based migrating group and requires that the O-O bond of molecular oxygen is not cleaved prior to substrate activation. No substrate: O-formyl-hydroxymethylphosphonate, (2S)-hydroxypropylphosphonate

719645

Streptomyces viridochromogenes

?

-

Acetylphosphate

-

Streptomyces viridochromogenes

(2R)-hydroxypropylphosphonate + O2

-

719645

Streptomyces viridochromogenes

2-oxopropylphosphonate + hydroxymethylphosphonate + acetate

substrate partitions between conversion to 2-oxopropylphosphonate and hydroxymethylphosphonate

-

?

1-hydroxy-2,2,2-trifluoroethylphosphonate + O2

-

719645

Streptomyces viridochromogenes

trifluoroacetylphosphonate

-

?

1-hydroxyethylphosphonate + O2

-

719645

Streptomyces viridochromogenes

acetylphosphate

-

?

2-hydroxyethylphosphonate + O2

-

719645

Streptomyces viridochromogenes

hydroxymethylphosphonate + formate

-

?

hydroxymethylphosphonate + O2

-

719645

Streptomyces viridochromogenes

phosphate + formate

-

?

additional information

results provide strong support for a mechanism that proceeds by hydroperoxylation followed by a Criegee rearrangement with a phosphorus-based migrating group and requires that the O-O bond of molecular oxygen is not cleaved prior to substrate activation. No substrate: O-formyl-hydroxymethylphosphonate, (2S)-hydroxypropylphosphonate

719645

Streptomyces viridochromogenes

?

-

745178

Peck

O-H activation by an unexpect ...

Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736

J. Am. Chem. Soc.

139

2045-2052

2017

-

1

-

1

-

1

-

1

-

2

-

4

-

1

-

4

1

-

1

-

1

-

1

-

1

-

2

-

1

-

4

1

-

1

-

745390

Peck

Go it alone four-electron oxi ...

Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736

J. Biol. Inorg. Chem.

22

381-394

2017

-

1

-

1

-

2

-

4

-

1

-

6

-

1

-

1

-

2

-

6

-

2

-

745162

Peck

A common late-stage intermedi ...

Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736

J. Am. Chem. Soc.

137

3217-3220

2015

-

1

-

1

-

1

-

2

-

4

-

1

-

2

-

1

-

1

-

1

-

1

-

2

-

1

-

2

-

1

-

720308

Du

Water-dependent reaction pathw ...

Streptomyces viridochromogenes

J. Phys. Chem. B

116

11837-11844

2012

-

1

-

2

-

2

-

718907

Peck

Mechanism and substrate recogn ...

Streptomyces viridochromogenes

Biochemistry

50

6598-6605

2011

-

4

-

6

-

1

-

2

-

2

-

4

-

6

-

2

-

2

-

6

719655

Whitteck

On the stereochemistry of 2-hy ...

Streptomyces viridochromogenes

J. Am. Chem. Soc.

133

4236-4239

2011

-

1

-

3

-

3

-

719648

Hirao

Ferric superoxide and ferric h ...

Streptomyces viridochromogenes

J. Am. Chem. Soc.

132

17901-17909

2010

-

1

-

1

-

1

-

1

-

1

-

719645

Whitteck

Hydroperoxylation by hydroxyet ...

Streptomyces viridochromogenes

J. Am. Chem. Soc.

131

16225-16232

2009

-

1

-

1

-

6

-

1

-

6

-

720539

Cicchillo

An unusual carbon-carbon bond ...

Streptomyces viridochromogenes

Nature

459

871-874

2009

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

Hydroperoxylation by hydroxyethylphosphonate dioxygenase

Data extracted from this reference: