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  • In Vivo Product
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  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
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Ligand L-pyrroline-5-carboxylate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

KEGG

Alanine, aspartate and glutamate metabolism, Arginine and proline metabolism, Biosynthesis of amino acids, Biosynthesis of secondary metabolites, Carbapenem biosynthesis

MetaCyc

(5R)-carbapenem carboxylate biosynthesis, ethene biosynthesis II (microbes), ethene biosynthesis IV (engineered), indolmycin biosynthesis, L-arginine degradation VI (arginase 2 pathway), L-arginine degradation XIII (reductive Stickland reaction), L-citrulline biosynthesis, L-Ndelta-acetylornithine biosynthesis, L-proline biosynthesis I (from L-glutamate), L-proline biosynthesis III (from L-ornithine), L-proline degradation I, peramine biosynthesis, proline to cytochrome bo oxidase electron transfer more

Show all BRENDA pathways known for L-pyrroline-5-carboxylate

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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

2.3.1.226

malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-5-carboxymethylproline + CO2

723203, 723252, 722646, 721285

-

2.3.1.226

malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-carboxymethylproline + CO2

721595, 722643

-

2.3.1.226

2 entries

2.3.1.271

acetyl-CoA + L-DELTA1-pyrroline 5-carboxylate + H2O = CoA + N-acetyl-glutamate-gamma-semialdehyde

748124

-

In Vivo Product in Enzyme-catalyzed Reactions (9 results)

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Show Natural Product (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.19

3 2-oxoglutarate + L-arginine + 3 O2 = 2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate

-

-

1.14.20.7

2-oxoglutarate + L-arginine + O2 = ethylene + succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O

-

-

1.14.20.7

2-oxoglutarate + L-arginine + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O

-

-

1.5.5.2

L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol

-

-

1.5.5.2

L-proline + acceptor + H2O = (S)-1-pyrroline-5-carboxylate + reduced acceptor

392555, 392556, 392560,

-

1.5.5.2

L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor

-

-

1.5.5.2

L-proline + oxidized phenazine methosulfate = (S)-1-pyrroline-5-carboxylate + reduced phenazine methosulfate

-

-

1.5.99.B2

L-proline + acceptor + H2O = (S)-1-pyrroline-5-carboxylate + reduced acceptor

392557, 392562, 392558, 392563, 392559

-

1.5.99.B2

L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor

-

-

1.14.20.7

2 entries

1.5.5.2

4 entries

1.5.99.B2

2 entries

Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Substrate (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.226

malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-5-carboxymethylproline + CO2

721595, 722026, 723203, 723252, 722646, 721285, 722643

-

2.3.1.226

malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-carboxymethylproline + CO2

721595, 722643

-

2.3.1.226

methylmalonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-6-methyl-5-carboxymethylproline + CO2

721595, 722643

-

2.3.1.271

acetyl-CoA + L-DELTA1-pyrroline 5-carboxylate + H2O = CoA + N-acetyl-glutamate-gamma-semialdehyde

748124

-

2.3.1.271

acetyl-CoA + L-DELTA1-pyrroline-5-carboxylate + H2O = CoA + N-acetyl-glutamate-gamma-semialdehyde

749164

-

2.3.1.226

3 entries

2.3.1.271

2 entries

Product in Enzyme-catalyzed Reactions (28 results)

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Show Product (28 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.19

3 2-oxoglutarate + L-arginine + 3 O2 = 2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate

-

-

1.14.20.7

2-oxoadipate + L-arginine + O2 = glutarate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O

-

-

1.14.20.7

2-oxoglutarate + L-arginine + O2 = ethylene + succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O

-

-

1.14.20.7

2-oxoglutarate + L-arginine + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate

-

-

1.14.20.7

2-oxoglutarate + L-arginine + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O

-

-

1.14.20.7

3 2-oxoglutarate + L-arginine + 3 O2 = 2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate

-

-

1.5.5.2

L-proline + 2,6-dichlorophenolindophenol + H2O = (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol

-

-

1.5.5.2

L-proline + 2,6-dichlorphenol-indophenol = (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol

-

-

1.5.5.2

L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol

-

-

1.5.5.2

L-proline + acceptor + H2O = (S)-1-pyrroline-5-carboxylate + reduced acceptor

392555, 392556, 392560,

-

1.5.5.2

L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor

-

-

1.5.5.2

L-proline + cytochrome c = (S)-1-pyrroline-5-carboxylate + reduced cytochrome c

-

-

1.5.5.2

L-proline + FAD + H2O = (S)-1-pyrroline-5-carboxylate + FADH2

-

-

1.5.5.2

L-proline + ferricyanide + H2O = (S)-1-pyrroline-5-carboxylate + ferrocyanide

-

-

1.5.5.2

L-proline + NAD+ + H2O = (S)-1-pyrroline-5-carboxylate + NADH

-

-

1.5.5.2

L-proline + NAD+ = (S)-1-pyrroline-5-carboxylate + NADH

-

-

1.5.5.2

L-proline + oxidized phenazine methosulfate = (S)-1-pyrroline-5-carboxylate + reduced phenazine methosulfate

-

-

1.5.99.B2

L-proline + 2,6-dichlorophenolindophenol + H2O = (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol

-

-

1.5.99.B2

L-proline + 2,6-dichlorophenolindophenol = (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol

-

-

1.5.99.B2

L-proline + acceptor + H2O = (S)-1-pyrroline-5-carboxylate + reduced acceptor

392557, , 392562, 392558, 392563, 392559

-

1.5.99.B2

L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor

-

-

1.5.99.B2

L-proline + cytochrome c + H2O = (S)-1-pyrroline-5-carboxylate + reduced cytochrome c

-

-

1.5.99.B2

L-proline + FAD = (S)-1-pyrroline-5-carboxylate + FADH2

-

-

1.5.99.B2

L-proline + H2O = (S)-1-pyrroline-5-carboxylate + H2O2

-

-

1.5.99.B2

L-proline + menadione = (S)-1-pyrroline-5-carboxylate + menadiol

-

-

1.5.99.B2

L-proline + oxidized 2,6-dichlorophenolindophenol + H2O = (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol

-

-

1.5.99.B2

L-proline + oxidized phenazine methosulfate = (S)-1-pyrroline-5-carboxylate + reduced phenazine methosulfate

-

-

1.5.99.B2

L-proline + p-iodonitrotetrazolium + H2O = (S)-1-pyrroline-5-carboxylate + reduced p-iodonitrotetrazolium

-

-

1.14.20.7

5 entries

1.5.5.2

11 entries

1.5.99.B2

11 entries

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

2.3.1.226

1.52

-

pH 7.8, 22°C

721595

K_M Value (3 results)

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Show KM Value (3 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.5.1.2

0.33

-

pH 6.5

392123

1.5.1.2

0.33

-

pH 8.0

392123

1.5.1.2

2 entries

2.3.1.226

0.0015

-

pH 7.8, 22°C

721595

References & Links

Literature References (18)

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Show Reference (18 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

392123

25881

Identity of proline dehydrogenase and delta1-pyrroline-5-carboxylic acid reductase in Clostridium sporogenes

1978

Costilow, R.N.; Cooper, D.

J. Bacteriol.

134

139-146

392555

3540963

Membrane association of proline dehydrogenase in Escherichia coli is redox dependent

1987

Wood, J.M.

Proc. Natl. Acad. Sci. USA

84

373-377

392556

6321477

Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association

1984

Graham, S.B.; Stephenson, J.T.; Wood, J.M.

J. Biol. Chem.

259

2656-2661

392557

6819140

Purification and properties of the bifunctional proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase from Pseudomonas aeruginosa

1982

Meile, L.; Leisinger, T.

Eur. J. Biochem.

129

67-75

392558

16662535

Proline oxidation in corn mitochondia

1982

Elthon, T.E.; Stewart, C.R.

Plant Physiol.

70

567-572

392559

7318831

Respiratory and enzymatic properties of squid heart mitochondria

1981

Mommsen, T.P.; Hochachka, P.W.

Eur. J. Biochem.

120

345-350

392560

355248

Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization

1978

Scarpulla, R.C.; Soffer, R.L.

J. Biol. Chem.

253

5997-6001

392562

5106921

Solubilization of proline dehydrogenase from rat liver mitochondria

1971

Kramar, R.

Hoppe-Seyler's Z. Physiol. Chem.

352

1267-1270

392563

5451904

The activities of proline dehydrogenase, glutamate dehydrogenase, aspartate-oxoglutarate aminotransferase and alanine-oxoglutarate aminotransferase in some insect flight muscles

1970

Crabtree, B.; Newsholme, E.A.

Biochem. J.

117

1019-1021

721285

18972478

Thioester hydrolysis and C-C bond formation by carboxymethylproline synthase from the crotonase superfamily

2008

Batchelar, E.T.; Hamed, R.B.; Ducho, C.; Claridge, T.D.; Edelmann, M.J.; Kessler, B.; Schofield, C.J.

Angew. Chem. Int. Ed. Engl.

47

9322-93225

721595

15595850

Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase superfamily

2004

Gerratana, B.; Arnett, S.O.; Stapon, A.; Townsend, C.A.

Biochemistry

43

15936-15945

722026

20162132

Carboxymethylproline synthase catalysed syntheses of functionalised N-heterocycles

2010

Hamed, R.B.; Mecinovic, J.; Ducho, C.; Claridge, T.D.; Schofield. C.J.

Chem. Commun. (Camb. )

46

1413-1415

722643

14625287

Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis

2004

Sleeman, M.C.; Schofield, C.J.

J. Biol. Chem.

279

6730-6736

722646

16096274

Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis

2005

Sleeman, M.C.; Sorensen, J.L.; Batchelar, E.T.; McDonough, M.A.; Schofield, C.J.

J. Biol. Chem.

280

34956-34965

723203

8939426

Analysis of bacterial carbapenem antibiotic production genes reveals a novel beta-lactam biosynthesis pathway

1996

McGowan, S.J.; Sebaihia, M.; Porter, L.E.; Stewart, G.S.; Williams, P.; Bycroft, B.W.; Salmond, G.P.

Mol. Microbiol.

22

415-426

723252

21505494

Stereoselective C-C bond formation catalysed by engineered carboxymethylproline synthases

2011

Hamed, R.B.; Gomez-Castellanos, J.R.; Thalhammer, A.; Harding, D.; Ducho, C.; Claridge, T.D.; Schofield. C.J.

Nat. Chem.

3

365-371

748124

26454877

Structure-based molecular design for thermostabilization of N-acetyltransferase Mpr1 involved in a novel pathway of L-arginine synthesis in yeast

2015

Nasuno, R.; Hirase, S.; Norifune, S.; Watanabe, D.; Takagi, H.

J. Biochem.

159

271-277

749164

23818613

Structural and functional analysis of the yeast n-Acetyltransferase mpr1 involved in oxidative stress tolerance via proline metabolism

2013

Nasuno, R.; Hirano, Y.; Itoh, T.; Hakoshima, T.; Hibi, T.; Takagi, H.

Proc. Natl. Acad. Sci. USA

110

11821-11826

Links to other databases for L-pyrroline-5-carboxylate

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Show Links (1 entry)

ChEBI

PubChem

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