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Ligand N3-fumaroyl-L-2,3-diaminopropanoic acid

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for N3-fumaroyl-L-2,3-diaminopropanoic acid

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.3.2.B15

ATP + (2E)-4-[[(2S)-2-amino-2-carboxyethyl]amino]-4-oxobut-2-enoate + L-isoleucine = ADP + phosphate + N-[(2S)-3-[[(2E)-4-amino-4-oxobut-2-enoyl]amino]-2-methylpropanoyl]-L-isoleucine

729202

-

6.3.2.B15

ATP + (2E)-4-[[(2S)-2-amino-2-carboxyethyl]amino]-4-oxobut-2-enoate + L-leucine = ADP + phosphate + N-[(2S)-3-[[(2E)-4-amino-4-oxobut-2-enoyl]amino]-2-methylpropanoyl]-L-leucine

729202

-

6.3.2.B15

ATP + (2E)-4-[[(2S)-2-amino-2-carboxyethyl]amino]-4-oxobut-2-enoate + L-valine = ADP + phosphate + N-[(2S)-3-[[(2E)-4-amino-4-oxobut-2-enoyl]amino]-2-methylpropanoyl]-L-valine

729202

-

6.3.2.B15

3 entries

Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Substrate (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.3.2.B15

ATP + (2E)-4-[[(2S)-2-amino-2-carboxyethyl]amino]-4-oxobut-2-enoate + L-isoleucine = ADP + phosphate + N-[(2S)-3-[[(2E)-4-amino-4-oxobut-2-enoyl]amino]-2-methylpropanoyl]-L-isoleucine

729202

-

6.3.2.B15

ATP + (2E)-4-[[(2S)-2-amino-2-carboxyethyl]amino]-4-oxobut-2-enoate + L-leucine = ADP + phosphate + N-[(2S)-3-[[(2E)-4-amino-4-oxobut-2-enoyl]amino]-2-methylpropanoyl]-L-leucine

729202

-

6.3.2.B15

ATP + (2E)-4-[[(2S)-2-amino-2-carboxyethyl]amino]-4-oxobut-2-enoate + L-valine = ADP + phosphate + N-[(2S)-3-[[(2E)-4-amino-4-oxobut-2-enoyl]amino]-2-methylpropanoyl]-L-valine

729202, 729882

-

6.3.2.B15

3 entries

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.6.1.16

-

639910, 639917

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

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Show Turnover Number (1 entry)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

6.3.2.B15

0.35

-

pH 8.0, 22°C

729882

K_M Value (1 result)

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Show KM Value (1 entry)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

6.3.2.B15

0.072

-

pH 8.0, 22°C

729882

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.6.1.16

0.008

-

pH 7.5, 37°C

639910

2.6.1.16

0.0551

-

pH 7.5, 37°C

639917

2.6.1.16

2 entries

References & Links

Literature References (4)

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Show Reference (4 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

639910

3082365

Inactivation of glucosamine-6-phosphate synthethase from Salmonella typhimurium LT2 by fumarolyl diaminopropanoic acid derivatives, a novel group of glutamine analogs

1985

Chmara, H.; Andruszkiewicz, R.; Borowski, E.

Biochim. Biophys. Acta

870

357-366

639917

3132968

Glucosamine synthetase from Escherichia coli: kinetic mechanism and inhibition by N3-fumaroyl-L-2,3-diaminopropionic derivatives

1988

Badet, B.; Vermoote, P.; Le Goffic, F.

Biochemistry

27

2282-2287

729202

19807062

The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics

2009

Hollenhorst, M.A.; Clardy, J.; Walsh, C.T.

Biochemistry

48

10467-10472

729882

20945916

Matthews, M.L.; Bollinger, J.M.Jr.; Kelleher, N.L.; Walsh, C.T.: The nonribosomal peptide synthetase enzyme DdaD tethers N(beta)-fumaramoyl-l-2,3-diaminopropionate for Fe(II)/alpha-ketoglutarate-dependent epoxidation by DdaC during dapdiamide antibiotic biosynthesis

2010

Hollenhorst, M.A.; Bumpus, S.B.

J. Am. Chem. Soc.

132

15773-15781

Links to other databases for N3-fumaroyl-L-2,3-diaminopropanoic acid

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Show Links (1 entry)

ChEBI

PubChem