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Ligand 1-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

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Natural Substrate (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.88

1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH

654887, 392061, 392062, 392058, 392059, 392060, 392064

-

1.5.1.2

1-pyrroline-5-carboxylate + NAD(P)H + H+ = L-proline + NAD(P)+

723917

-

1.5.1.2

1-pyrroline-5-carboxylate + NADH + H+ = L-proline + NAD+

743355, 762678

-

1.5.1.2

1-pyrroline-5-carboxylate + NADPH + H+ = L-proline + NADP+

676952, 676969, 743355, 762678

-

1.5.1.2

DELTA1-pyrroline-5-carboxylate + NADH + H+ = L-proline + NAD+

704292

-

1.5.1.2

pyrroline-5-carboxylate + NAD(P)H + H+ = L-proline + NAD(P)+

392133, 392143, 390310, 392107, 392106, 392108, 392110, 392121, 392115

-

1.5.1.2

5 entries

2.3.1.271

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

747802

-

In Vivo Product in Enzyme-catalyzed Reactions (4 results)

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Show Natural Product (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.2

L-Pro + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H

0

-

1.5.1.2

L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+

0

-

1.5.1.2

L-proline + NADP+ = 1-pyrroline-5-carboxylate + NADPH + H+

0

-

1.5.1.2

3 entries

2.6.1.13

L-ornithine + 2-oxoglutarate = DELTA1-pyrroline-5-carboxylate + L-glutamate

0

-

Substrate in Enzyme-catalyzed Reactions (18 results)

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Show Substrate (18 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.86

pyrroline-5-carboxylate + NADPH + H+ = ? + NADP+

738989

-

1.2.1.88

1-pyrroline-5-carboxylate + NAD(P)+ + H2O = L-glutamate + NAD(P)H

654887

-

1.2.1.88

1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH

392044, 392045, 392051, 392039, 654887, 392042, 392047, 392055, 392053, 392056, 392041, 392049, 392061, 392062, 392058, 392059, 740489, 392048, 392060, 392065, 392064

-

1.2.1.88

1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH + H+

675402, 392047, 392041, 392050, 392060, 740734, 740744

-

1.2.1.88

1-pyrroline-5-carboxylate + NADH + H+ = L-proline + NAD+

740061

-

1.2.1.88

1-pyrroline-5-carboxylate + NADP+ + H2O = L-glutamate + NADPH

740489

-

1.2.1.88

1-pyrroline-5-carboxylate + NADP+ + H2O = L-glutamate + NADPH + H+

392053, 392062, 392041, 392065, 675402

-

1.5.1.2

1-pyrroline-5-carboxylate + NAD(P)H + H+ = L-proline + NAD(P)+

392038, 392133, 392143, 392147, 392066, 392121, 689728, 392119, 392132, 171971, 392113, 723917, 726110, 392130, 392108, 392146, 392126, 392047, 392131, 390310, 392123, 392111

-

1.5.1.2

1-pyrroline-5-carboxylate + NAD(P)H = L-proline + NAD(P)+

701063

-

1.5.1.2

1-pyrroline-5-carboxylate + NADH + H+ = L-proline + NAD+

392126, 392140, 392128, 392111, 392112, 392119, 392117, 392133, 392107, 392110, 392125, 725183, 390310, 723917, 723922, 676952, 392146, 392123, 686421, 392130, 392108, 740763, 763270, 763322, 740491, 741069, 763462, 743355, 762678

-

1.5.1.2

1-pyrroline-5-carboxylate + NADH = L-proline + NAD+

762678

-

1.5.1.2

1-pyrroline-5-carboxylate + NADPH + H+ = L-proline + NADP+

392126, 392111, 392138, 392133, 392110, 390310, 723922, 676952, 740763, 763322, 676969, 740491, 741069, 762709, 763462, 743355, 762678

-

1.5.1.2

1-pyrroline-5-carboxylate + NADPH = L-proline + NADP+

762678

-

1.5.1.2

DELTA1-pyrroline-5-carboxylate + NADH + H+ = L-proline + NAD+

704292

-

1.5.1.2

pyrroline-5-carboxylate + NAD(P)H + H+ = L-proline + NAD(P)+

392133, 392143, 392125, 390310, 392107, 392106, 392108, 392110, 392121, 392115

-

1.2.1.88

6 entries

1.5.1.2

8 entries

1.5.1.20

1-pyrroline-5-carboxylate + NADH + H+ = L-proline + NAD+

392155

-

1.5.1.21

DELTA1-pyrroline-5-carboxylate + NADPH + H+ = ?

392169

-

2.3.1.271

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

748318, 747764, 747802, 749156

-

Product in Enzyme-catalyzed Reactions (26 results)

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Show Product (26 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.2

L-Pro + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H

0

-

1.5.1.2

L-Pro + NAD+ = 1-pyrroline-5-carboxylate + NADH

0

-

1.5.1.2

L-Pro + NADP+ = 1-pyrroline-5-carboxylate + NADPH

0

-

1.5.1.2

L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H

0

-

1.5.1.2

L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+

0

-

1.5.1.2

L-proline + NAD+ = 1-pyrroline-5-carboxylate + NADH + H+

0

-

1.5.1.2

L-proline + NADP+ = 1-pyrroline-5-carboxylate + NADPH + H+

0

-

1.5.5.2

L-proline + oxidized dichlorophenolindophenol = 1-pyrroline-5-carboxylate + reduced dichlorophenolindophenol

0

-

1.5.5.2

L-proline + 2,6-dichlorophenolindophenol + H2O = DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol

0

-

1.5.99.B2

L-proline + oxidized dichlorophenolindophenol = 1-pyrroline-5-carboxylate + reduced dichlorophenolindophenol

0

-

1.5.99.B2

L-proline + oxidized ferrocenecarboxylic acid = 1-pyrroline-5-carboxylate + reduced ferrocenecarboxylic acid

0

-

1.5.99.B2

L-hydroxyproline + 2,6-dichlorophenolindophenol + H2O = DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol

0

-

1.5.99.B2

L-proline + 2,6-dichlorophenolindophenol + H2O = DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol

0

-

1.5.99.B2

L-proline + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium + H2O = DELTA1-pyrroline-5-carboxylate + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium

0

-

1.5.99.B2

L-proline + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium = DELTA1-pyrroline-5-carboxylate + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium

0

-

1.5.99.B2

L-proline + 4-iodonitrotetrazolium violet + H2O = DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet

0

-

1.5.99.B2

L-proline + coenzyme Q1 + H2O = DELTA1-pyrroline-5-carboxylate + reduced coenzyme Q1

0

-

1.5.99.B2

L-proline + ferricyanide = DELTA1-pyrroline-5-carboxylate + ferrocyanide

0

-

2.6.1.13

D-ornithine + 2-oxoglutarate = glutamate + DELTA1-pyrroline-5-carboxylate

0

-

2.6.1.13

L-ornithine + 2-oxoglutarate = DELTA1-pyrroline-5-carboxylate + glutamate

0

-

2.6.1.13

L-ornithine + 2-oxoglutarate = DELTA1-pyrroline-5-carboxylate + L-glutamate

0, 637123, 637111, 637137, 637109, 637126, 637121, 637130, 637115, 637120, 637098

-

2.6.1.13

L-ornithine + 2-oxoglutarate = glutamate + DELTA1-pyrroline-5-carboxylate

0

-

2.6.1.13

L-ornithine + 2-oxoglutarate = L-glutamate + DELTA1-pyrroline-5-carboxylate

0

-

2.6.1.13

L-ornithine + glyoxylate = DELTA1-pyrroline-5-carboxylate + glycine

0

-

2.6.1.13

L-ornithine + pyruvate = DELTA1-pyrroline-5-carboxylate + L-alanine

0

-

2.6.1.13

ornithine + oxaloacetate = DELTA1-pyrroline-5-carboxylate + L-aspartate

0

-

1.5.1.2

7 entries

1.5.5.2

2 entries

1.5.99.B2

9 entries

2.6.1.13

8 entries

Inhibitor in Enzyme-catalyzed Reactions (4 results)

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Show Inhibitors (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.2

substrate inhibition

392108

-

2.6.1.16

competitive with respect to L-glutamine

639926

-

6.3.4.2

weak

648963

-

6.3.4.2

0.125 mM, complete inhibition of ammonium chloride-dependent CTP synthesis

660794

-

6.3.4.2

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (24 results)

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Show Turnover Number (24 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.2.1.88

1.5

-

pH 7.5, 20°C

740061

1.2.1.88

1.6

-

pH 7.4, 50°C

675402

1.2.1.88

5.16

-

pH 7.5, 21°C

740734

1.2.1.88

25

-

-

392059

1.5.1.2

0.00983

-

cofactor NADPH

676952

1.5.1.2

0.08

-

mutant R119C, cosubstrate NADH, pH 7.5, 37°C

762678

1.5.1.2

0.08

-

pH 7.5, 37°C, recombinant mutant R119C, with NADH

762678

1.5.1.2

0.13

-

mutant R119C, cosubstrate NADPH, pH 7.5, 37°C

762678

1.5.1.2

0.13

-

pH 7.5, 37°C, recombinant mutant R119C, with NADPH

762678

1.5.1.2

1

-

pH 7, 28°C

762709

1.5.1.2

3.1

-

mutant R251C, cosubstrate NADPH, pH 7.5, 37°C

762678

1.5.1.2

3.1

-

pH 7.5, 37°C, recombinant mutant R251C, with NADPH

762678

1.5.1.2

3.2

-

mutant R251C, cosubstrate NADH, pH 7.5, 37°C

762678

1.5.1.2

3.2

-

pH 7.5, 37°C, recombinant mutant R251C, with NADH

762678

1.5.1.2

14

-

mutant T238A, wild-type, pH 7.5, 37°C

740763

1.5.1.2

26

-

pH 7.5, 37°C, recombinant wild-type enzyme, with NADPH

762678

1.5.1.2

26

-

wild-type, cosubstrate NADPH, pH 7.5, 37°C

762678

1.5.1.2

31

-

cosubstrate NADPH, wild-type, pH 7.5, 37°C

740763

1.5.1.2

61.3

-

pH 7.5, 37°C, recombinant wild-type enzyme, with NADH

762678

1.5.1.2

61.3

-

wild-type, cosubstrate NADH, pH 7.5, 37°C

762678

1.5.1.2

387.3

-

cofactor NADH

676952

1.5.1.2

451.7

-

cofactor NADPH

676952

1.5.1.2

1270

-

-

392113

1.2.1.88

4 entries

1.5.1.2

19 entries

2.3.1.271

121

-

at pH 7.5 and 30°C

749156

K_M Value (72 results)

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Show KM Value (72 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.88

0.037

-

pH 7.4, 50°C

675402

1.2.1.88

0.062

-

with NADP+

392053

1.2.1.88

0.09

-

-

392039

1.2.1.88

0.104

-

pH 7.5, 20°C

740061

1.2.1.88

0.109

-

-

392059

1.2.1.88

0.17

-

-

392039

1.2.1.88

0.18

-

-

392047

1.2.1.88

0.2

-

isoform B, with NADP+

392065

1.2.1.88

0.265

-

cosubstrate NADP+, pH 7.5, 35°C

740489

1.2.1.88

0.29

-

with NAD+

392053

1.2.1.88

0.3

-

isoform A, with NADP+

392065

1.2.1.88

0.3

-

isoform B, with NAD+

392065

1.2.1.88

0.33

-

isoform A, with NAD+

392065

1.2.1.88

0.35

-

-

392050

1.2.1.88

0.358

-

cosubstrate NAD+, pH 7.5, 35°C

740489

1.2.1.88

0.42

-

isoform I

392060

1.2.1.88

0.42

-

with NADP+

392041

1.2.1.88

0.46

-

-

392062

1.2.1.88

0.75

-

with NAD+

392041

1.2.1.88

1.22

-

isoform II

392060

1.2.1.88

2

-

pH 7.5, 21°C

740734

1.5.1.2

0.02

-

cosubstrate NADPH, pH 7.5, 35°C

740491

1.5.1.2

0.022

-

cosubstrate NADPH

392112

1.5.1.2

0.024

0.025

-

392111

1.5.1.2

0.0277

-

pH 7, 28°C

762709

1.5.1.2

0.04

-

cofactor NADH

676952

1.5.1.2

0.047

-

cofactor NADPH

676952

1.5.1.2

0.051

-

cosubstrate NADPH

392112

1.5.1.2

0.08

-

-

392119

1.5.1.2

0.09

-

-

392130

1.5.1.2

0.09

-

with NADH

390310

1.5.1.2

0.096

-

cofactor NADPH, pH 7.8, 35°C

741069

1.5.1.2

0.12

-

with NADPH

392110, 390310

1.5.1.2

0.125

-

-

392117

1.5.1.2

0.14

-

with NADH

392126

1.5.1.2

0.15

-

with NADPH

392126

1.5.1.2

0.154

-

-

392125

1.5.1.2

0.17

-

-

392108

1.5.1.2

0.184

-

apparent value, with NADPH as cosubstrate, at pH 7.5 and 37°C

723922

1.5.1.2

0.19

-

-

392146

1.5.1.2

0.2

-

with NADH

392110

1.5.1.2

0.21

-

cosubstrate NADH

392112

1.5.1.2

0.24

-

cosubstrate NADH, pH 7.5, 35°C

740491

1.5.1.2

0.273

-

cosubstrate NADH, pH 7.5, 30°C

763462

1.5.1.2

0.317

-

pH 7.5, 37°C, recombinant mutant R119C, with NADH

762678

1.5.1.2

0.32

-

mutant R119C, cosubstrate NADH, pH 7.5, 37°C

762678

1.5.1.2

0.33

-

mutant R119C, cosubstrate NADPH, pH 7.5, 37°C

762678

1.5.1.2

0.334

-

pH 7.5, 37°C, recombinant mutant R119C, with NADPH

762678

1.5.1.2

0.34

-

-

392140

1.5.1.2

0.349

-

apparent value, with NADH as cosubstrate, at pH 7.5 and 37°C

723922

1.5.1.2

0.37

-

with NADPH

392138

1.5.1.2

0.44

-

-

392128

1.5.1.2

0.45

-

with NADPH

392133

1.5.1.2

0.53

-

with NADH

392133

1.5.1.2

0.62

-

-

392047

1.5.1.2

0.62

-

cosubstrate NADH

392111, 392112

1.5.1.2

0.667

-

cosubstrate NADPH, wild-type, pH 7.5, 37°C

740763

1.5.1.2

0.915

-

cofactor NADH, pH 7.8, 35°C

741069

1.5.1.2

0.949

-

pH 7.5, 37°C, recombinant wild-type enzyme, with NADPH

762678

1.5.1.2

0.99

-

wild-type, cosubstrate NADPH, pH 7.5, 37°C

762678

1.5.1.2

1.053

-

cosubstrate NADPH, pH 7.5, 30°C

763462

1.5.1.2

1.315

-

pH 7.5, 37°C, recombinant mutant R251C, with NADH

762678

1.5.1.2

1.32

-

mutant R251C, cosubstrate NADH, pH 7.5, 37°C

762678

1.5.1.2

1.499

-

pH 7.5, 37°C, recombinant mutant R251C, with NADPH

762678

1.5.1.2

1.5

-

mutant R251C, cosubstrate NADPH, pH 7.5, 37°C

762678

1.5.1.2

1.509

-

pH 7.5, 37°C, recombinant wild-type enzyme, with NADH

762678

1.5.1.2

1.51

-

wild-type, cosubstrate NADH, pH 7.5, 37°C

762678

1.5.1.2

1.62

1.64

-

392111

1.5.1.2

2.887

-

mutant T238A, wild-type, pH 7.5, 37°C

740763

1.2.1.88

21 entries

1.5.1.2

48 entries

1.5.1.21

0.4

-

-

392169

2.3.1.271

7.01

-

at pH 7.5 and 30°C

749156

2.6.1.13

1.4

-

-

637115

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.6.1.16

0.023

-

-

639926

References & Links

Literature References (93)

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Show Reference (93 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

171971

6075416

The biosynthesis of proline by Tetrahymena pyriformis

1967

Hill, D.L.; Chambers, P.

Biochim. Biophys. Acta

148

435-447

390310

114173

Biosynthesis of proline in Pseudomonas aeruginosa. Properties of gamma-glutamyl phosphate reductase and 1-pyrroline-5-carboxylate reductase

1979

Krishna, R.V.; Beilstein, P.; Leisinger, T.

Biochem. J.

181

223-230

392038

13502341

Enzymatic synthesis of L-pipecolic acid and L-proline

1957

Meister, A.; Radhakrishnan, A.N.; Buckley, S.D.

J. Biol. Chem.

229

789-800

392039

2211729

Pyrroline 5-carboxylate dehydrogenase of the mitochondrial matrix of rat liver. Purification, physical and kinetic characteristics

1990

Small, W.C.; Jones, M.E.

J. Biol. Chem.

265

18668-18672

392041

-

Crystallization and characterization of 1-pyrroline-5-carboxylate dehydrogenase from Bacillus sphaericus

1987

Isobe, K.; Matsuzawa, T.; Soda, K.

Agric. Biol. Chem.

51

1947-1953

392042

2883912

A specific radiochemical assay for pyrroline-5-carboxylate dehydrogenase

1987

Small, C.; Jones, M.E.

Anal. Biochem.

161

380-386

392044

6270101

Enzymatic properties of the purified putA protein from Salmonella typhimurium

1981

Menzel, R.; Roth, J.

J. Biol. Chem.

256

9762-9766

392045

6270100

Purification of the putA gene product. A bifunctional membrane-bound protein from Salmonella typhimurium responsible for the two-step oxidation of proline to glutamate

1981

Menzel, R.; Roth, J.

J. Biol. Chem.

256

9755-9761

392047

901423

Enzymes metabolizing delta1-pyrroline-5-carboxylate in rat tissues

1977

Herzfeld, A.; Mezl, V.A.; Knox, W.E.

Biochem. J.

166

95-103

392048

16659283

DELTA1-pyrroline-5-carboxylic acid dehydrogenase in barley, a proline-accumulating species

1975

Boggess, S.F.; Paleg, L.G.; Aspinall, D.

Plant Physiol.

56

259-262

392049

-

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