print visible entries

print all entries

Ligand 2-hydroxyethylphosphonate

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 2-hydroxyethylphosphonate

close all tables

open all tables

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (5 results)

top print hide

Show Natural Substrate (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.72

2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate

764974, 745162, 745178, 763810, 745390

-

1.13.11.73

2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3-

745162, 745390, 764510, 764974

6b9t, 3D-view

2.1.1.308

(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin = (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin

703345, 703183

-

2.1.1.308

S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate = 5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate

729108

-

2.1.1.308

2 entries

2.7.7.104

2-hydroxyethylphosphonate + CTP = cytidine 5'-[[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate] + diphosphate

755682

-

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

top print hide

Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.309

phosphonoacetaldehyde + NADH + H+ = 2-hydroxyethylphosphonate + NAD+

0

-

1.1.99.B6

phosphonoacetaldehyde + reduced acceptor = 2-hydroxyethylphosphonate + acceptor

0

-

Substrate in Enzyme-catalyzed Reactions (11 results)

top print hide

Show Substrate (11 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.309

2-hydroxyethylphosphonate + NAD+ = phosphonoacetaldehyde + NADH + H+

712363

-

1.1.99.B6

2-hydroxyethylphosphonate + NADP+ = phosphonoacetaldehyde + NADPH + H+

712363

-

1.13.11.72

(R)-2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate

719655

-

1.13.11.72

(S)-2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate

719655

-

1.13.11.72

2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate

764974, 718907, 719645, 745162, 745178, 763810, 745390, 720539, 720308, 719655

-

1.13.11.73

(R)-2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3-

719659

6b9t, 3D-view

1.13.11.73

(S)-2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3-

719659

6b9t, 3D-view

1.13.11.73

2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3-

745162, 745390, 764510, 764974, 721059, 719659

6b9t, 3D-view

2.1.1.308

(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin = (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin

704215, 705861, 703345, 703183, 705300, 704807

-

2.1.1.308

S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate = 5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate

729108

-

1.13.11.72

3 entries

1.13.11.73

3 entries

2.1.1.308

2 entries

2.7.7.104

2-hydroxyethylphosphonate + CTP = cytidine 5'-[[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate] + diphosphate

755682

-

Product in Enzyme-catalyzed Reactions (3 results)

top print hide

Show Product (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.309

phosphonoacetaldehyde + NADH + H+ = 2-hydroxyethylphosphonate + NAD+

0

-

1.1.1.309

phosphonoacetaldehyde + NADPH + H+ = 2-hydroxyethylphosphonate + NADP+

0

-

1.1.1.309

2 entries

1.1.99.B6

phosphonoacetaldehyde + reduced acceptor = 2-hydroxyethylphosphonate + acceptor

0

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

top print hide

Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.11.1.1

competitive inhibitor

246535

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

top print hide

Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

1.13.11.73

6b9t, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (5 results)

top print hide

Show Turnover Number (5 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.11.72

0.35

-

wild-type, pH 7.5, 20°C

718907

1.13.11.72

0.81

-

mutant R90K, pH 7.5, 20°C

718907

1.13.11.73

0.17

-

temperature not specified in the publication, pH not specified in the publication

719659

1.13.11.73

0.17

-

temperature not specified in the publication, pH not specified in the publication

719659

1.13.11.73

0.18

-

temperature not specified in the publication, pH not specified in the publication

719659

1.13.11.72

2 entries

1.13.11.73

3 entries

K_M Value (7 results)

top print hide

Show KM Value (7 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.72

0.0098

-

wild-type, pH 7.5, 20°C

718907

1.13.11.72

0.06

-

mutant R90K, pH 7.5, 20°C

718907

1.13.11.72

0.69

-

mutant R90A, pH 7.5, 20°C

718907

1.13.11.72

0.8

-

mutant Y98F, pH 7.5, 20°C

718907

1.13.11.73

0.0045

-

temperature not specified in the publication, pH not specified in the publication

719659

1.13.11.73

0.0065

-

temperature not specified in the publication, pH not specified in the publication

719659

1.13.11.73

0.0071

-

temperature not specified in the publication, pH not specified in the publication

719659

1.13.11.72

4 entries

1.13.11.73

3 entries

References & Links

Literature References (23)

top print hide

Show Reference (23 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

246535

1605625

Investigation of the substrate binding and catalytic groups of the P-C bond cleaving enzyme, phosphonoacetaldehyde hydrolase

1992

Olsen, D.B.; Hepburn, T.W.; Lee, S.l.; Martin, B.M.; Mariano, P.S.; Dunaway-Mariano, D.

Arch. Biochem. Biophys.

296

144-151

703183

17220970

New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin

2007

Woodyer, R.D.; Li, G.; Zhao, H.; van der Donk, W.A.

Chem. Commun. (Camb. )

4

359-361

703345

19297239

Anaerobic functionalization of unactivated C-H bonds

2009

Booker, S.J.

Curr. Opin. Chem. Biol.

13

58-73

704215

1468993

Studies on the biosynthesis of fosfomycin. 4. The biosynthetic origin of the methyl group of fosfomycin

1992

Kuzuyama, T.; Hidaka, T.; Kamigiri, K.; Imai, S.; Seto, H.

J. Antibiot.

45

1812-1814

704807

-

Biosynthesis of natural products with a P-C bond. Part 8: on the origin of the oxirane oxygen atom of fosfomycin in Streptomyces fradiae

1991

Hammerschmidt, F.

J. Chem. Soc. Perkin Trans.

1

1993-1996

705300

-

Biosynthesis of natural products with a P-C Bond. 7. Synthesis of [1,1-2H2]-, [2,2-2H2]-, (R)- and (S)-[2 H1](2-hydroxyethyl)phosphonic acid and (R,S)-[1-2H1](1,2-dihydroxyethyl)phosphonic acid and incorporation studies into fosfomycin in Streptomyces fradiae

1991

Hammerschmidt, F.; Kählig, H.

J. Org. Chem.

56

2364-2370

705861

10584333

Bioactive natural products with carbon-phosphorus bonds and their biosynthesis

1999

Seto, H.; Kuzuyama, T.

Nat. Prod. Rep.

16

589-596

712363

18544530

Biosynthesis of 2-hydroxyethylphosphonate, an unexpected intermediate common to multiple phosphonate biosynthetic pathways

2008

Shao, Z.; Blodgett, J.A.V.; Circello, B.T.; Eliot, A.C.; Woodyer, R.; Li, G.; van der Donk, W.A.; Metcalf, W.W.; Zhao, H.

J. Biol. Chem.

283

23161-23168

718907

21711001

Mechanism and substrate recognition of 2-hydroxyethylphosphonate dioxygenase

2011

Peck, S.C.; Cooke, H.A.; Cicchillo, R.M.; Malova, P.; Hammerschmidt, F.; Nair, S.K.; van der Donk, W.A.

Biochemistry

50

6598-6605

719645

19839620

Hydroperoxylation by hydroxyethylphosphonate dioxygenase

2009

Whitteck, J.T.; Cicchillo, R.M.; van der Donk, W.A.

J. Am. Chem. Soc.

131

16225-16232

719655

21381767

On the stereochemistry of 2-hydroxyethylphosphonate dioxygenase

2011

Whitteck, J.T.; Malova, P.; Peck, S.C.; Cicchillo, R.M.; Hammerschmidt, F.; van der Donk, W.A.

J. Am. Chem. Soc.

133

4236-4239

719659

22957470

Mechanistic investigation of methylphosphonate synthase, a non-heme iron-dependent oxygenase

2012

Cooke, H.A.; Peck, S.C.; Evans, B.S.; van der Donk, W.A.

J. Am. Chem. Soc.

134

15660-15663

720308

22950439

Water-dependent reaction pathways: an essential factor for the catalysis in HEPD enzyme

2012

Du, L.; Gao, J.; Liu, Y.; Liu, C.

J. Phys. Chem. B

116

11837-11844

720539

19516340

An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis

2009

Cicchillo, R.M.; Zhang, H.; Blodgett, J.A.; Whitteck, J.T.; Li, G.; Nair, S.K.; van der Donk, W.A.; Metcalf, W.W.

Nature

459

871-874

721059

22936780

Synthesis of methylphosphonic acid by marine microbes: A source for methane in the aerobic ocean

2012

Metcalf, W.; Griffin, B.; Cicchillo, R.; Gao, J.; Janga, S.; Cooke, H.; Circello, B.; Evans, B.; Martens-Habbena, W.; Stahl, D.; Van Der Donk, W.

Science

337

1104-1107

729108

24370735

Initial characterization of Fom3 from Streptomyces wedmorensis: The methyltransferase in fosfomycin biosynthesis

2014

Allen, K.D.; Wang, S.C.

Arch. Biochem. Biophys.

543

67-73

745162

25699631

A common late-stage intermediate in catalysis by 2-hydroxyethyl-phosphonate dioxygenase and methylphosphonate synthase

2015

Peck, S.C.; Chekan, J.R.; Ulrich, E.C.; Nair, S.K.; van der Donk, W.A.

J. Am. Chem. Soc.

137

3217-3220

745178

28092705

O-H activation by an unexpected ferryl intermediate during catalysis by 2-hydroxyethylphosphonate dioxygenase

2017

Peck, S.C.; Wang, C.; Dassama, L.M.; Zhang, B.; Guo, Y.; Rajakovich, L.J.; Bollinger, J.M.; Krebs, C.; van der Donk, W.A.

J. Am. Chem. Soc.

139

2045-2052

745390

27783267

Go it alone four-electron oxidations by mononuclear non-heme iron enzymes

2017

Peck, S.C.; van der Donk, W.A.

J. Biol. Inorg. Chem.

22

381-394

755682

28727444

Fosfomycin biosynthesis via transient cytidylylation of 2-hydroxyethylphosphonate by the bifunctional Fom1 enzyme

2017

Cho, S.H.; Kim, S.Y.; Tomita, T.; Shiraishi, T.; Park, J.S.; Sato, S.; Kudo, F.; Eguchi, T.; Funa, N.; Nishiyama, M.; Kuzuyama, T.

ACS Chem. Biol.

12

2209-2215

763810

-

Computational evidence for the enzymatic transformation of 2-hydroxypropylphosphonate to methylphosphonate

2018

Li, Y.; Wang, X.; Zhang, R.; Wang, J.; Yang, Z.; Du, L.; Tang, X.; Zhang, Q.; Wang, W.

ACS Earth Space Chem.

2

888-894

764510

31926045

How to produce methane precursor in the upper ocean by an untypical non-heme Fe-dependent methylphosphonate synthase?

2020

Yan, J.F.; Chen, S.L.

ChemPhysChem

21

385-396

764974

31132257

Fenton-derived OH radicals enable the MPnS enzyme to convert 2-hydroxyethylphosphonate to methylphosphonate Insights from ab initio QM/MM MD simulations

2019

Wang, B.; Cao, Z.; Rovira, C.; Song, J.; Shaik, S.

J. Am. Chem. Soc.

141

9284-9291

Links to other databases for 2-hydroxyethylphosphonate

top print hide

Show Links (1 entry)

ChEBI

PubChem