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Ligand N-acetylmuramate 6-phosphate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.105

N-acetyl-D-muramate 6-phosphate + H2O = N-acetyl-D-muramate + phosphate

750237

-

4.2.1.126

N-acetylmuramate 6-phosphate + H2O = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate

729247

-

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

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.192

[protein]-Npi-phospho-L-histidine + N-acetylmuramate[side 1] = [protein]-L-histidine + N-acetylmuramate 6-phosphate[side 2]

0

-

4.2.1.126

(R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H2O

0

-

Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.105

N-acetyl-D-muramate 6-phosphate + H2O = N-acetyl-D-muramate + phosphate

743209, 750237

-

4.2.1.126

N-acetylmuramate 6-phosphate + H2O = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate

712299, 714166, 715354, 715365, 729247, 748107

-

4.2.1.126

N-acetylmuramate 6-phosphate + H2O = D-lactate + N-acetyl-D-glucosamine 6-phosphate

715356, 715477

-

4.2.1.126

N-acetylmuramate 6-phosphate + H2O = N-acetyl-D-glucosamine 6-phosphate + D-lactate

714685

-

4.2.1.126

3 entries

Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.192

[protein]-Npi-phospho-L-histidine + N-acetylmuramate[side 1] = [protein]-L-histidine + N-acetylmuramate 6-phosphate[side 2]

0

-

4.2.1.126

(R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H2O

0

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.1.3.105

0.88

-

at pH 7.6 and 22°C

750237

3.1.3.105

0.88

-

pH 7.6, 22°C

743209

4.2.1.126

0.0005

-

mutant enzyme E83A, at 30°C in 60 mM Trien-HCl buffer (pH 8.0)

714166

4.2.1.126

0.0028

-

mutant enzyme E114Q, at 30°C in 60 mM Trien-HCl buffer (pH 8.0)

714166

4.2.1.126

0.79

-

mutant enzyme D115N, at 30°C in 60 mM Trien-HCl buffer (pH 8.0)

714166

4.2.1.126

5.7

-

wild type enzyme, at 30°C in 60 mM Trien-HCl buffer (pH 8.0)

714166

3.1.3.105

2 entries

4.2.1.126

4 entries

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.1.3.105

0.31

-

at pH 7.6 and 22°C

750237

3.1.3.105

0.31

-

pH 7.6, 22°C

743209

4.2.1.126

0.32

-

mutant enzyme E114Q, at 30°C in 60 mM Trien-HCl buffer (pH 8.0)

714166

4.2.1.126

0.83

-

mutant enzyme D115N, at 30°C in 60 mM Trien-HCl buffer (pH 8.0)

714166

4.2.1.126

1.2

-

wild type enzyme, at 30°C in 60 mM Trien-HCl buffer (pH 8.0)

714166

3.1.3.105

2 entries

4.2.1.126

3 entries

References & Links

Literature References (11)

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Show Reference (11 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

712299

20400549

Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase

2010

Litzinger, S.; Duckworth, A.; Nitzsche, K.; Risinger, C.; Wittmann, V.; Mayer, C.

J. Bacteriol.

192

3132-3143

714166

18837509

Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling

2008

Hadi, T.; Dahl, U.; Mayer, C.; Tanner, M.E.

Biochemistry

47

11547-11558

714685

18049859

N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism

2008

Jaeger, T.; Mayer, C.

Cell. Mol. Life Sci.

65

928-939

715354

15901686

Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate

2005

Uehara, T.; Suefuji, K.; Valbuena, N.; Meehan, B.; Donegan, M.; Park, J.T.

J. Bacteriol.

187

3643-3649

715356

16452451

MurQ etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall

2006

Uehara, T.; Suefuji, K.; Jaeger, T.; Mayer, C.; Park, J.T.

J. Bacteriol.

188

1660-1662

715365

20139182

The N-acetylmuramic acid 6-phosphate etherase gene promotes growth and cell differentiation of cyanobacteria under light-limiting conditions

2010

Jiang, H.; Kong, R.; Xu, X.

J. Bacteriol.

192

2239-2245

715477

15983044

Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli etherase

2005

Jaeger, T.; Arsic, M.; Mayer, C.

J. Biol. Chem.

280

30100-30106

729247

24251551

Structure of MurNAc 6-phosphate hydrolase (MurQ) from Haemophilus influenzae with a bound inhibitor

2013

Hadi, T.; Hazra, S.; Tanner, M.E.; Blanchard, J.S.

Biochemistry

52

9358-9366

743209

28351914

The N-acetylmuramic acid 6-phosphate phosphatase MupP completes the Pseudomonas peptidoglycan recycling pathway leading to intrinsic fosfomycin resistance

2017

Borisova, M.; Gisin, J.; Mayer, C.

mBio

8

e00092

748107

27601356

Identification of a novel N-acetylmuramic acid transporter in Tannerella forsythia

2016

Ruscitto, A.; Hottmann, I.; Stafford, G.P.; Schaeffer, C.; Mayer, C.; Sharma, A.

J. Bacteriol.

198

3119-3125

750237

28505548

Enzymatic synthesis and semi-preparative isolation of N-acetylmuramic acid 6-phosphate

2017

Unsleber, S.; Borisova, M.; Mayer, C.

Carbohydr. Res.

445

98-103

Links to other databases for N-acetylmuramate 6-phosphate

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Show Links (1 entry)

ChEBI

PubChem

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