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Ligand (S)-1-pyrroline-5-carboxylate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

(5R)-carbapenem carboxylate biosynthesis, proline metabolism

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 (S)-1-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 (29 results)

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Show Product (29 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

4.2.1.172

trans-4-hydroxy-L-proline = (S)-1-pyrroline-5-carboxylate + H2O

-

-

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 (S)-1-pyrroline-5-carboxylate

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ChEBI

PubChem