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Ligand 5-L-glutamyl-4-nitroanilide

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Basic Ligand Information

Molecular Structure

Picture of 5-L-glutamyl-4-nitroanilide (click for magnification)

Molecular Formula

BRENDA Name

InChIKey

C₁₁H₁₃N₃O₅

5-L-glutamyl-4-nitroanilide

WMZTYIRRBCGARG-VIFPVBQESA-N

Synonyms:

(gamma-L-glutamyl)-4-nitroanilide, 4-L-Glutamyl-4-nitroanilide, 5-L-glutamyl-4-nitroaniline, 5-L-glutamyl-L-p-nitroanilide, 5-L-glutamyl 4-nitroanilide, gamma-glutamyl-4-nitroanilide, gamma-L-glutamyl-4-nitroanilide, gamma-L-glutamyl-L-p-nitroanilide, gamma-L-Glutamyl-p-nitroanilide, L-gamma-glutamine-4-nitroanilide, L-gamma-glutamyl-4-nitroanilide, L-gamma-glutamyl-p-nitroanilide, L-gamma -glutamyl-p-nitroanilide, L-gamma-glutamyl p-nitroanilide, L-glutamic acid gamma-(4-nitroanilide)

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (127 results)

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Show Substrate (127 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.2

(gamma-L-glutamyl)-4-nitroanilide + glycylglycine = 4-nitroaniline + gamma-glutamylglycylglycine

756547, 756619, 756753

2.3.2.2

5-L-glutamyl 4-nitroanilide + Gly-Gly = 4-nitroaniline + 5-L-glutamyl-Gly-Gly

689579

2.3.2.2

5-L-glutamyl-4-nitroanilide + (S)-2-aminobutyrate = 4-nitroaniline + N-[(1S)-1-carboxypropyl]-L-glutamine

487923, 487947

2.3.2.2

5-L-glutamyl-4-nitroanilide + 1-amino-cyclopropane-1-carboxylic acid = 4-nitroaniline + 5-L-glutamyl-1-amino-cyclopropane-1-carboxylic acid

672686

2.3.2.2

5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide = 5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline

487919, 487928, 487923, 487926, 487903

2.3.2.2

5-L-glutamyl-4-nitroanilide + acceptor = 4-nitroaniline + 5-L-glutamyl-acceptor

487948

2.3.2.2

5-L-glutamyl-4-nitroanilide + Ala-Ala-Ala = 4-nitroaniline + 5-L-glutamyl-Ala-Ala-Ala

676991

2.3.2.2

5-L-glutamyl-4-nitroanilide + Arg = 4-nitroaniline + 5-L-glutamyl-Arg

676991, 675471, 672686

2.3.2.2

5-L-glutamyl-4-nitroanilide + Asn = 4-nitroaniline + 5-L-glutamyl-Asn

675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + Asp = 4-nitroaniline + 5-L-glutamyl-Asp

672686, 675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + citrulline = 4-nitroaniline + 5-L-glutamyl-citrulline

487914, 487907

2.3.2.2

5-L-glutamyl-4-nitroanilide + Cys = 4-nitroaniline + 5-L-glutamyl-Cys

675471, 672686

2.3.2.2

5-L-glutamyl-4-nitroanilide + Cys-Gly = 4-nitroaniline + 5-L-glutamyl-Cys-Gly

672686

2.3.2.2

5-L-glutamyl-4-nitroanilide + DL-Phe = 4-nitroaniline + 5-L-glutamyl-DL-Phe

675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + ethylamine = N-ethyl-L-glutamine + 4-nitroaniline

671541

2.3.2.2

5-L-glutamyl-4-nitroanilide + ethylamine = theanine + 4-nitroaniline

676992

2.3.2.2

5-L-glutamyl-4-nitroanilide + Glu = 4-nitroaniline + 5-L-glutamyl-Glu

672686, 675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + Gly = 4-nitroaniline + 5-L-glutamyl-Gly

658567, 672686, 675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + Gly-Gly = 4-nitroaniline + 5-L-glutamyl-Gly-Gly

658567, 675471, 704637, 672838, 703332, 703335, 674593, 676991, 672686, 689061, 673912, 703990, 704335

2.3.2.2

5-L-glutamyl-4-nitroanilide + Gly-Gly-Ala = 4-nitroaniline + 5-L-glutamyl-Gly-Gly-Ala

676991

2.3.2.2

5-L-glutamyl-4-nitroanilide + Gly-Gly-Gly = 4-nitroaniline + 5-L-glutamyl-Gly-Gly-Gly

676991

2.3.2.2

5-L-glutamyl-4-nitroanilide + glycine = 4-nitroaniline + 5-L-glutamyl-glycine

487947, 487950, 487951, 487920, 487922, 487923, 487926

2.3.2.2

5-L-glutamyl-4-nitroanilide + glycyl-glycine = 4-nitroaniline + 5-L-glutamyl-glycyl-glycine

686496

2.3.2.2

5-L-glutamyl-4-nitroanilide + glycyl-L-proline = 4-nitroaniline + 5-L-glutamyl-glycyl-L-proline

487942

2.3.2.2

5-L-glutamyl-4-nitroanilide + glycylglycine = 4-nitroaniline + 5-L-glutamyl-glycylglycine

736220, 735923, 736623, 736144

2.3.2.2

5-L-glutamyl-4-nitroanilide + glycylglycine = 4-nitroaniline + 5-L-glutamylglycylglycine

487931, 487943, 487922, 487944, 487945, 657592, 487902, 487935, 487937, 487938, 487941, 487942, 487949, 487956, 487961, 487963, 659102, 487934, 487916, 487918, 487919, 487969, 660051, 487907, 487908, 487911, 487924, 487921, 487926, 487946, 487953, 487947, 487950, 487951, 487972, 487966, 487932, 487914, 487920, 487923, 487903, 658768

2.3.2.2

5-L-glutamyl-4-nitroanilide + glycylglycine = 5-L-glutamyl-glycylglycine + 4-nitroaniline

720135, 707820, 719952, 718951, 717083

2.3.2.2

5-L-glutamyl-4-nitroanilide + H2O = 4-nitroaniline + Glu

658567, 660108, 659787

2.3.2.2

5-L-glutamyl-4-nitroanilide + H2O = 4-nitroaniline + L-glutamate

674593, 487963, 487925, 487967

2.3.2.2

5-L-glutamyl-4-nitroanilide + H2O = L-glutamate + 4-nitroaniline

676991, 689061

2.3.2.2

5-L-glutamyl-4-nitroanilide + H2O = p-nitroaniline + Glu

658768

2.3.2.2

5-L-glutamyl-4-nitroanilide + His = 4-nitroaniline + 5-L-glutamyl-His

675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + Ile = 4-nitroaniline + 5-L-glutamyl-Ile

676991, 675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Ala = 4-nitroaniline + 5-L-glutamyl-L-Ala

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-alanine = 4-nitroaniline + 5-L-glutamyl-L-alanine

487902, 487938, 487914, 487969, 487923, 487924, 487947, 487950, 487951, 487920, 487926

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-alanylglycine = 4-nitroaniline + 5-L-glutamyl-L-alanylglycine

487969

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Arg = 4-nitroaniline + 5-L-glutamyl-L-Arg

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-arginine = 4-nitroaniline + 5-L-glutamyl-L-arginine

487914, 487924, 487926, 487947, 487950, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Asn = 4-nitroaniline + 5-L-glutamyl-L-Asn

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Asp = 4-nitroaniline + 5-L-glutamyl-L-Asp

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-asparagine = 4-nitroaniline + 5-L-glutamyl-L-asparagine

487944, 487938, 487926, 487950

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-aspartate = 4-nitroaniline + 5-L-glutamyl-L-aspartate

487936, 487969, 487926, 487947, 487950, 487951, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Cys = 4-nitroaniline + 5-L-glutamyl-L-Cys

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-cysteine = 4-nitroaniline + 5-L-glutamyl-L-cysteine

487936, 487924, 487947, 487950, 487951

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-cysteinylglycine = 4-nitroaniline + glutathione

487930

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-cystine = 4-nitroaniline + 5-L-glutamyl-L-cystine

487944, 487902, 487932, 487914, 487931, 487936, 487950, 487929, 487930, 487903

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Gln = 4-nitroaniline + 5-L-glutamyl-L-Gln

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Glu = 4-nitroaniline + 5-L-glutamyl-L-Glu

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-glutamate = 4-nitroaniline + 5-L-glutamyl-L-glutamate

487938, 487914, 487969, 487923, 487924, 487926, 487947, 487950, 487951

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-glutamine = 4-nitroaniline + 5-L-glutamyl-L-glutamine

487902, 487937, 487938, 487942, 487914, 487930, 487936, 487969, 487907, 487911, 487923, 487924, 487926, 487947, 487951, 487903, 487920, 487899

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-His = 4-nitroaniline + 5-L-glutamyl-L-His

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-histidine = 4-nitroaniline + 5-L-glutamyl-L-histidine

487926, 487947, 487950, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-hydroxyproline = 4-nitroaniline + 5-L-glutamyl-L-hydroxyproline

487947, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Ile = 4-nitroaniline + 5-L-glutamyl-L-Ile

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-isoleucine = 4-nitroaniline + 5-L-glutamyl-L-isoleucine

487926, 487950, 487951, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Leu = 4-nitroaniline + 5-L-glutamyl-L-Leu

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-leucine = 4-nitroaniline + 5-L-glutamyl-L-leucine

487926, 487947, 487950, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-leucyl-L-alanine = 4-nitroaniline + 5-L-glutamyl-L-leucyl-L-alanine

487942

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Lys = 4-nitroaniline + 5-L-glutamyl-L-Lys

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-lysine = 4-nitroaniline + 5-L-glutamyl-L-lysine

487914, 487924, 487926, 487947, 487950, 487951, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Met = 4-nitroaniline + 5-L-glutamyl-L-Met

660108, 658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-methioninamide = 4-nitroaniline + 5-L-glutamyl-L-methioninamide

657955

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-methionine = 4-nitroaniline + 5-L-glutamyl-L-methionine

487902, 487938, 487914, 487936, 487969, 487907, 487911, 487924, 487947, 487951, 487922, 487923, 487920, 487926, 487899

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-methionyl(2,2,2-trifluoroethylamide) = 4-nitroaniline + 5-L-glutamyl-L-methionyl(2,2,2-trifluoroethylamide)

657955

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-methionyl(2-fluoroethylamide) = 4-nitroaniline + 5-L-glutamyl-L-methionyl(2-fluoroethylamide)

657955

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-methionyl(3,3,3-trifluoropropylamide) = 4-nitroaniline + 5-L-glutamyl-L-methionyl(3,3,3-trifluoropropylamide)

657955

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-methionylethylamide = 4-nitroaniline + 5-L-glutamyl-L-methionylethylamide

657955

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-methionylpropylamide = 4-nitroaniline + 5-L-glutamyl-L-methionylpropylamide

657955

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Phe = 4-nitroaniline + 5-L-glutamyl-L-Phe

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-phenylalanine = 4-nitroaniline + 5-L-glutamyl-L-phenylalanine

487969, 487924, 487926, 487947, 487950, 487951, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Pro = 4-nitroaniline + 5-L-glutamyl-L-Pro

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-proline = 4-nitroaniline + 5-L-glutamyl-L-proline

487923, 487947, 487951

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Ser = 4-nitroaniline + 5-L-glutamyl-L-Ser

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-serine = 4-nitroaniline + 5-L-glutamyl-L-serine

487938, 487923, 487947, 487950, 487951, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Thr = 4-nitroaniline + 5-L-glutamyl-L-Thr

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-threonine = 4-nitroaniline + 5-L-glutamyl-L-threonine

487947, 487951, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Trp = 4-nitroaniline + 5-L-glutamyl-L-Trp

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-tryptophan = 4-nitroaniline + 5-L-glutamyl-L-tryptophan

487947, 487950, 487951

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-tyrosine = 4-nitroaniline + 5-L-glutamyl-L-tyrosine

675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Val = 4-nitroaniline + 5-L-glutamyl-L-Val

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-valine = 4-nitroaniline + 5-L-glutamyl-L-valine

487926, 487947, 487950, 487951, 487920

2.3.2.2

5-L-glutamyl-4-nitroanilide + Leu = 4-nitroaniline + 5-L-glutamyl-Leu

675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + Lys = 4-nitroaniline + 5-L-glutamyl-Lys

676991, 675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + Met = 4-nitroaniline + 5-L-glutamyl-Met

676991, 687267, 672686, 675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + Pro = 4-nitroaniline + 5-L-glutamyl-Pro

675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + S-alkylcysteine sulfoxide = 4-nitroaniline + 5-L-glutamyl-S-alkylcysteine sulfoxide

487947

2.3.2.2

5-L-glutamyl-4-nitroanilide + Ser = 4-nitroaniline + 5-L-glutamyl-Ser

675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + taurine = 4-nitroaniline + 5-L-glutamyl-taurine

658567

2.3.2.2

5-L-glutamyl-4-nitroanilide + Thr = 4-nitroaniline + 5-L-glutamyl-Thr

676991, 675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + Tyr = 4-nitroaniline + 5-L-glutamyl-Tyr

675471

2.3.2.2

5-L-glutamyl-4-nitroanilide + Val = 4-nitroaniline + 5-L-glutamyl-Val

675471

2.3.2.2

gamma-glutamyl-4-nitroanilide + hydroxamate = 4-nitroaniline + gamma-L-glutamylhydroxamate

756223

2.3.2.2

gamma-L-glutamyl-4-nitroanilide + Gly-Gly = 4-nitroaniline + gamma-L-glutamyl-Gly-Gly

727437

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + ethylamine = 4-nitroaniline + 5-L-glutamyl-ethylamine

756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + glycine = 4-nitroaniline + 5-L-glutamyl-glycine

756967, 757413

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + glycine methylester = 4-nitroaniline + 5-L-glutamyl-glycyl methylester

752957

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + glycylglycine = 4-nitroaniline + 5-L-glutamyl-glycyl-glycine

754814

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + glycylglycine = 4-nitroaniline + 5-L-glutamyl-glycylglycine

756934, 757049, 752957, 757548, 758292, 754222, 756966, 756938, 757270, 757413, 757351, 756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + glycylglycine methylester = 4-nitroaniline + 5-L-glutamyl-glycylglycine methylester

752957

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-alanine = 4-nitroaniline + 5-L-glutamyl-L-alanine

756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-arginine = 4-nitroaniline + 5-L-glutamyl-L-arginine

757413, 756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-asparagine = 4-nitroaniline + 5-L-glutamyl-L-asparagine

757413, 756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-aspartate = 4-nitroaniline + 5-L-glutamyl-L-aspartate

756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-glutamate = 4-nitroaniline + 5-L-glutamyl-L-glutamate

757270, 756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-glutamine = 4-nitroaniline + 5-L-glutamyl-L-glutamine

756967, 757270

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-histidine = 4-nitroaniline + 5-L-glutamyl-L-histidine

757413, 756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-isoleucine = 4-nitroaniline + 5-L-glutamyl-L-isoleucine

757413, 756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-leucine = 4-nitroaniline + 5-L-glutamyl-L-leucine

757413, 756967, 757270

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-lysine = 4-nitroaniline + 5-L-glutamyl-L-lysine

757413, 756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-methionine = 4-nitroaniline + 5-L-glutamyl-L-methionine

757413, 756967, 757270

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-phenylalanine = 4-nitroaniline + 5-L-glutamyl-L-phenylalanine

757413, 756967, 755925, 755923

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-proline = 4-nitroaniline + 5-L-glutamyl-L-proline

757413

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-serine = 4-nitroaniline + 5-L-glutamyl-L-serine

756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-threonine = 4-nitroaniline + 5-L-glutamyl-L-threonine

757413, 756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-tryptophan = 4-nitroaniline + 5-L-glutamyl-L-tryptophan

757413, 756967

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-valine = 4-nitroaniline + 5-L-glutamyl-L-valine

757413, 756967, 757270

2.6.1.16

L-gamma-glutamyl-p-nitroanilide + D-fructose 6-phosphate = ?

671896

2.6.1.16

L-gamma-glutamyl-p-nitroanilide + H2O = L-glutamine + p-nitroaniline

685109, 671896, 673687

L-gamma-glutamine-4-nitroanilide + H2O = L-glutamate + 4-nitroaniline

750749

3.4.19.13

L-gamma-glutamyl-4-nitroanilide + H2O = 4-nitroaniline + L-glutamate

757413

3.4.19.9

5-L-glutamyl-4-nitroanilide + H2O = L-glutamic acid + 4-nitroaniline

702486

3.4.19.9

L-glutamic acid gamma-(4-nitroanilide) + H2O = L-glutamic acid + 4-nitroaniline

L-gamma-glutamyl-4-nitroanilide + H2O = L-glutamate + 4-nitroaniline

732844

3.5.1.2

gamma-L-glutamyl-4-nitroanilide + H2O = L-glutamate 4-nitroanilide + NH3

733562

3.5.1.2

L-gamma-glutamyl-4-nitroanilide + H2O = L-glutamate 4-nitroanilide + NH3

733239

3.5.1.2

L-gamma-glutamyl-p-nitroanilide + H2O = ?

L-gamma-glutamyl p-nitroanilide + H2O = L-glutamate + p-nitroaniline

661225, 661368

Product in Enzyme-catalyzed Reactions (2 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.3.2.9

5-L-glutamyl-5-L-glutamyl-4-nitroanilide = 5-oxoproline + 5-L-glutamyl-4-nitroanilide

4.3.2.9

5-L-glutamyl-L-5-L-glutamyl-L-4-nitroanilide = 5-L-oxoproline + 5-L-glutamyl-L-p-nitroanilide

487978, 487979, 487982, 487975, 487986

4.3.2.9

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (37 results)

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EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.3.2.2

0.105

671541

2.3.2.2

0.49

mutant S463T, pH 9.0, 37Â°C

703990

2.3.2.2

0.62

wild-type, pH 9.0, 37Â°C

703990

2.3.2.2

1.42

mutant T399S, pH 8.0, 40Â°C

703335

2.3.2.2

1.7

recombinant mutant R109E, pH 9.0, 60Â°C

754222

2.3.2.2

1.7

recombinant mutant R109F, pH 9.0, 60Â°C

754222

2.3.2.2

8.3

recombinant mutant R109L, pH 9.0, 60Â°C

754222

2.3.2.2

8.93

recombinant mutant N450K, pH 9.0, 40Â°C

756966

2.3.2.2

37Â°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT I

672686

2.3.2.2

37Â°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II

672686

2.3.2.2

16.04

recombinant wild-type enzyme, pH 9.0, 40Â°C

756966

2.3.2.2

21.7

recombinant mutant R109M, pH 9.0, 60Â°C

754222

2.3.2.2

21.74

recombinant mutant N450Q, pH 9.0, 40Â°C

756966

2.3.2.2

24.24

mutant T417S, pH 8.0, 40Â°C

703335

2.3.2.2

37Â°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT B

672686

2.3.2.2

37Â°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT A

672686

2.3.2.2

43.33

wild-type enzyme

658768

2.3.2.2

56.33

mutant enzyme D445A

658768

2.3.2.2

recombinant mutant R109S, pH 9.0, 60Â°C

754222

2.3.2.2

in 1 mM MgCl2, 50 mM Tris-HCl buffer (pH 8.0), at 40Â°C

718951

2.3.2.2

106.7

recombinant wild-type enzyme, pH 9.0, 60Â°C

754222

2.3.2.2

109.5

wild-type, pH 8.0, 40Â°C

703335

2.3.2.2

123.65

recombinant mutant N450A, pH 9.0, 40Â°C

756966

2.3.2.2

175.52

recombinant mutant N450D, pH 9.0, 40Â°C

756966

2.3.2.2

305

recombinant mutant R109K, pH 9.0, 60Â°C

754222

2.6.1.16

0.00092

wild-type with N-terminal His-tag, pH 7.5, 25Â°C

671896

2.6.1.16

0.0075

residues 1-345, His-tagged glutamine amide-hydrolysing domain, pH 7.5, 25Â°C

671896

2.6.1.16

0.012

wild-type, pH 7.5, 25Â°C

671896

2.6.1.16

0.0123

reaction mixture contains 1 mM L-gamma-glutamyl-p-nitroanilide, 1 mM EDTA, 1 mM DTT and the appropriately diluted enzyme preparation in 20 mM HEPES buffer (pH 7.5) at 25Â°C

671896

2.6.1.16

0.013

wild-type with C-terminal His-tag, pH 7.5, 25Â°C

671896

2.6.1.16

0.13

mutant V605L, 37Â°C

673687

2.6.1.16

0.15

mutant A602L, 37Â°C

673687

2.6.1.16

0.17

wild-type, 37Â°C

673687

2.6.1.16

0.5

mutant W74L, 37Â°C

673687

2.6.1.16

0.67

mutant W74F, 37Â°C

673687

2.6.1.16

0.68

mutant W74A, 37Â°C

207.8

at pH 8.0 and 37Â°C

732844

K_M Value (76 results)

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EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.2.2

0.0109

37Â°C, pH 8.0, transpeptidase reaction with Gly-Gly

0.0125

0.0125

37Â°C, pH 8.0, hydrolysis

674593

2.3.2.2

0.0143

pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme H368S

0.021

0.021

pH 7.4, 37Â°C

757548

2.3.2.2

0.024

37Â°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II

672686

2.3.2.2

0.025

pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme H368S

727437

2.3.2.2

0.025

pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme Y327N

727437

2.3.2.2

0.045

wild-type, pH 9.0, 37Â°C

703990

2.3.2.2

0.046

37Â°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT I

672686

2.3.2.2

0.058

mutant S463T, pH 9.0, 37Â°C

703990

2.3.2.2

0.067

pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme Y327N

727437

2.3.2.2

0.07

wild-type, pH 8.0, 40Â°C

703335

2.3.2.2

0.073

hydrolysis

676991

2.3.2.2

0.08

in 1 mM MgCl2, 50 mM Tris-HCl buffer (pH 8.0), at 40Â°C

718951

2.3.2.2

0.09

mutant T417S, pH 8.0, 40Â°C

703335

2.3.2.2

0.1

pH 7.0, temperature not specified in the publication, hydrolytic activity, wild-type enzyme

727437

2.3.2.2

0.11

mutant T399S, pH 8.0, 40Â°C

703335

2.3.2.2

0.123

pH 9.6, 37Â°C, recombinant enzyme

757270

2.3.2.2

0.2

pH 8.0, 37Â°C, native extracellular enzyme

754814

2.3.2.2

0.214

recombinant extracellular enzyme, pH 9.0, 40Â°C

757049

2.3.2.2

0.22

monomeric 30-kDa enzyme, at pH 11.0, in the presence of subtilisin, at 80Â°C

707820

2.3.2.2

0.25

heterodimeric 67-kDa enzyme, at pH 8.0, in the absence of subtilisin, at 60Â°C

707820

2.3.2.2

0.3

recombinant mutant R109F, pH 9.0, 60Â°C

754222

2.3.2.2

0.4

recombinant mutant R109E, pH 9.0, 60Â°C

754222

2.3.2.2

0.4

recombinant mutant R109S, pH 9.0, 60Â°C

754222

2.3.2.2

0.4

recombinant wild-type enzyme, pH 9.0, 60Â°C

754222

2.3.2.2

0.42

recombinant wild-type enzyme, pH 9.0, 40Â°C

756966

2.3.2.2

0.579

recombinant immobilized modified wild-type enzyme MTWs-GGT-Phar, pH 8.0, 37Â°C

756934

2.3.2.2

0.58

recombinant mutant N450D, pH 9.0, 40Â°C

756966

2.3.2.2

0.58

recombinant mutant N450Q, pH 9.0, 40Â°C

756966

2.3.2.2

0.597

recombinant free wild-type enzyme GGT, pH 8.0, 37Â°C

756934

2.3.2.2

0.69

recombinant mutant N450A, pH 9.0, 40Â°C

756966

2.3.2.2

0.7

recombinant mutant R109K, pH 9.0, 60Â°C

754222

2.3.2.2

0.74

at pH 8.0 and 37Â°C

735923

2.3.2.2

0.75

hydrolysis

689061

2.3.2.2

0.76

recombinant mutant N450K, pH 9.0, 40Â°C

756966

2.3.2.2

0.84

reaction in the presence of 20 mM glycylglycine

689061

2.3.2.2

0.879

recombinant immobilized wild-type enzyme, MTWs-GGT, pH 8.0, 37Â°C

756934

2.3.2.2

1.1

mutant enzyme N266Q, at 37Â°C, pH 7.4

719952

2.3.2.2

1.2

mutant enzyme N95Q, at 37Â°C, pH 7.4

719952

2.3.2.2

1.2

pH 7.4, 37Â°C, recombinant enzyme

758292

2.3.2.2

1.3

mutant enzyme N120Q, at 37Â°C, pH 7.4

719952

2.3.2.2

1.3

mutant enzyme N230Q, at 37Â°C, pH 7.4

719952

2.3.2.2

1.3

mutant enzyme N297Q, at 37Â°C, pH 7.4

719952

2.3.2.2

1.3

mutant enzyme N344Q, at 37Â°C, pH 7.4

719952

2.3.2.2

1.3

mutant enzyme N511Q, at 37Â°C, pH 7.4

719952

2.3.2.2

1.3

wild type enzyme, at 37Â°C, pH 7.4

1.8

3.6

pH 8.0, 37Â°C

757351

2.3.2.2

4.3

37Â°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT B

672686

2.3.2.2

4.4

37Â°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT A

672686

2.3.2.2

5.2

monomeric 30-kDa enzyme, at pH 8.0, in the absence of subtilisin, at 60Â°C

707820

2.3.2.2

8.2

recombinant mutant R109L, pH 9.0, 60Â°C

754222

2.3.2.2

10.4

wild-type enzyme

658768

2.3.2.2

10.6

recombinant mutant R109M, pH 9.0, 60Â°C

15.3

mutant enzyme D445A

658768

2.6.1.16

0.0064

mutant W74F, 37Â°C

673687

2.6.1.16

0.05

wild-type, 37Â°C

673687

2.6.1.16

0.1

mutant W74L, 37Â°C

673687

2.6.1.16

0.2

mutant W74A, 37Â°C

673687

2.6.1.16

0.29

mutant V605L, 37Â°C

673687

2.6.1.16

0.31

residues 1-345, His-tagged glutamine amide-hydrolysing domain, pH 7.5, 25Â°C

671896

2.6.1.16

0.36

mutant A602L, 37Â°C

673687

2.6.1.16

0.64

wild-type with C-terminal His-tag, pH 7.5, 25Â°C

671896

2.6.1.16

0.67

reaction mixture contains 1 mM L-gamma-glutamyl-p-nitroanilide, 1 mM EDTA, 1 mM DTT and the appropriately diluted enzyme preparation in 20 mM HEPES buffer (pH 7.5) at 25Â°C

671896

2.6.1.16

0.67

wild-type, pH 7.5, 25Â°C

671896

2.6.1.16

1.8

both wild-type and mutant S243E, 37Â°C, pH 7.5

685109

2.6.1.16

12.2

wild-type with N-terminal His-tag, pH 7.5, 25Â°C

671896

3.4.19.9

0.0076

pH 7.8, 52Â°C

702486

3.4.19.9

0.0076

Vmax: 0.36 micromol/min/mg

0.273

at pH 8.0 and 37Â°C

3.8

5.92

References & Links

Literature References (116)

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Show Reference (116 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

487899

Partial purification and characterization of gamma-glutamyl transpeptidase from rat kidney

1986

Kimm, S.W.; Kim, E.G.; Park, S.C.

Korean J. Biochem.

135-143

487902

6150450

Solubilization and some properties of gamma-glutamyltransferase from human brain microvessels

1984

Vesely, J.; Cernoch, M.

Neurochem. Res.

927-934

487903

Studies on the properties of the variants of gamma-glutamyl transpeptidase in human urine

1982

Rambabu, K.; Pattabiraman, T.N.

J. Biosci.

287-294

487907

Some properties of gamma-glutamyltransferase from hog small intestine

1981

Nakamura, Y.; Kato, H.; Suzuki, F.; Nagata, Y.

Biomed. Res.

509-516

487908

6114882

Purification and properties of gamma-glutamyl transpeptidase from bovine parotid gland

1981

Hata, K.; Hayakawa, M.; Abiko, Y.; Takiguchi, H.

Int. J. Biochem.

681-692

487911

42549

gamma-Glutamyl transpeptidase of bovine ciliary body: purification and properties

1979

Das, N.D.; Shichi, H.

Exp. Eye Res.

109-121

487914

39603

Purification and comparison of several catalytic parameters of the gamma-glutamyltranspeptidase of rat mammary adenocarcinoma (13762) and of normal rat mammary gland

1979

Jaken, S.; Mason, M.

Biochim. Biophys. Acta

568

331-338

487916

6102912

Latent active site in rat-kidney gamma-glutamyl transpeptidase. The refolding process of the large subunit and characterization of the renatured enzyme

1980

Horiuchi, S.; Inoue, M.; Morino, Y.

Eur. J. Biochem.

105

93-102

487918

6139125

Phenobarbital and related compounds as novel inhibitors of gamma-glutamyltranspeptidase

1983

Sachdev, G.P.; Leahy, D.S.; Chace, K.V.

Biochim. Biophys. Acta

749

125-129

487919

6128031

Purification and characterization of gamma-glutamyltransferase from rat pancreas

1982

Takahashi, S.; Steinman, H.M.; Ball, D.

Biochim. Biophys. Acta

707

66-73

487920

6152628

Purification and properties of gamma-glutamyl transpeptidase from rat deciduoma

1984

Tarachand, U.

J. Appl. Biochem.

278-288

487921

6113845

Some kinetic properties of gamma-glutamyltransferase from rabbit liver

1981

Bagrel, D.; Petitclerc, C.; Schiele, F.; Siest, G.

Biochim. Biophys. Acta

658

220-231

487922

36916

Identification, partial purification and biochemical characterization of gamma-glutamyltranspeptidase present as a membrane component in skimmed milk and milk fat-globule membranes, and in mammary-tumour virus from the milk of infected mice

1979

FranÃ¾ois, C.; Calberg-Bacq, C.M.; Gosselin, L.; Kozma, S.; Osterrieth, P.M.

Biochim. Biophys. Acta

567

106-115

487923

32176

Purification and enzymatic properties of gamma-glutamyltransferase from bovine colostrum

1978

Yasumoto, K.; Iwami, K.; Fushiki, T.; Mitsuda, H.

J. Biochem.

1227-1236

487924

6135696

Purification and properties of bovine liver gamma-glutamyltransferase

1983

Furukawa, M.; Higashi, T.; Tateishi, N.; Ochi, K.; Sakamoto, Y.

J. Biochem.

839-846

487925

7566

Kinetic studies of sheep kidney gamma-glutamyl transpeptidase

1976

Karkowsky, A.M.; Bergamini, M.V.W.; Orlowski, M.

J. Biol. Chem.

251

4736-4743

487926

1275

gamma-Glutamyl transpeptidase of sheep-kidney cortex. Isolation, catalytic properties and dissociation into two polypeptide chains

1976

Zelazo, P.; Orlowski, M.

Eur. J. Biochem.

147-155

487928

6126192

Kinetics of the conversion of leukotriene C by gamma-glutamyl transpeptidase

1982

Ãrning, L.; HammarstrÃ¶m, S.

Biochem. Biophys. Res. Commun.

106

1304-1309

487929

6127596

gamma-Glutamyl transpeptidase, a leukotriene metabolizing enzyme

1982

BernstrÃ¶m, K.; Orning, L.; HammarstrÃ¶m, S.

Methods Enzymol.

38-45

487930

2868391

gamma-Glutamyl transpeptidase: kinetics and mechanism

1985

Allison, D.

Methods Enzymol.

113

419-437

487931

2868390

gamma-Glutamyl transpeptidase from kidney

1985

Tate, S.S.; Meister, A.

Methods Enzymol.

113

400-419

487932

gamma-Glutamyltransferase. (gamma-Glutamyl)-peptide:amino acid gamma-glutamyltransferase, EC 2.3.2.2. 1. General

1983

Shaw, L.M.

Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )

349-352

487934

gamma-Glutamyltransferase. (gamma-Glutamyl)-peptide:amino acid gamma-glutamyltransferase, EC 2.3.2.2. 3. IFCC reference method (provisional)

1983

Shaw, L.M.; Stromme, J.H.

Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )

357-364

487935

6112969

gamma-Glutamyl transpeptidase from WI-38 fibroblasts: purification and active site modification studies

1981

Takahashi, S.; Zukin, R.S.; Steinman, H.M.

Arch. Biochem. Biophys.

207

87-95

487936

2859051

Purification of gamma-glutamyltransferase by phenyl boronate affinity chromatography. Studies on the acceptor specificity of transpeptidation by rat kidney gamma-glutamyltransferase

1985

Cook, N.D.; Peters, T.J.

Biochim. Biophys. Acta

828

205-212

487937

4442

Studies of human kidney gamma-glutamyl transpeptidase. Purification and structural, kinetic and immunological properties

1976

Miller, S.P.; Awasthi, Y.C.; Srivastava, S.K.

J. Biol. Chem.

251

2271-2278

487938

19463

Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit

1977

Tate, S.S.; Ross, M.E.

J. Biol. Chem.

252

6042-6045

487941

18197

Purification and some properties of gamma-glutamyltransferase from human liver

1977

Huseby, N.

Biochim. Biophys. Acta

483

46-56

487942

18198

Partial purification and some properties of gamma-glutamyl transpeptidase from human bile

1977

Indirani, N.; Hill, P.G.

Biochim. Biophys. Acta

483

57-62

487943

1371053

Purification and properties of gamma-glutamyltranspeptidase from Bacillus subtilis (natto)

1991

Ogawa, Y.; Hosoyama, H.; Hamano, M.; Motai, H.

Agric. Biol. Chem.

2971-2977

487944

2877974

gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties

1986

Suzuki, H.; Kumagai, H.; Tochikura, T.

J. Bacteriol.

168

1325-1331

487945

2877975

gamma-Glutamyltranspeptidase from Escherichia coli K-12: formation and localization

1986

Suzuki, H.; Kumagai, H.; Tochikura, T.

J. Bacteriol.

168

1332-1335

487946

6148333

Purification and properties of gamma-glutamyltranspeptidase from Proteus mirabilis

1984

Nakayama, R.; Kumagai, H.; Tochikura, T.

J. Bacteriol.

160

341-346

487947

Properties of gamma-glutamyltransferase from Lentinus edodes

1975

Iwami, K.; Yasumoto, K.; Nakamura, K.; Mitsuda, H.

Agric. Biol. Chem.

1933-1940

487948

Reactivity of Lentinus gamma-glutamyltransferase with lentinic acid as the principal endogenous substrate

1975

Iwami, K.; Yasumoto, K.; Nakamura, K.; Mitsuda, H.

Agric. Biol. Chem.

1941-1946

487949

35101

Isolation of anthglutin, an inhibitor of gamma-glutamyl transpeptidase from Penicillum oxalicum

1979

Minato, S.

Arch. Biochem. Biophys.

192

235-240

487950

Purification and properties of gamma-glutamyltranspeptidase from Penicillium roqueforti IFO 4622

1990

Tomita, K.; Yano, T.; Tsuchida, T.; Kumagai, H.; Tochikura, T.

J. Ferment. Bioeng.

128-130

487951

2870692

Partial purification and properties of gamma-glutamyltranspeptidase from mycelia of Morchella esculenta

1986

Moriguchi, M.; Yamada, M.; Suenaga, S.; Tanaka, H.; Wakasugi, A.; Hatanaka, S.I.

Arch. Microbiol.

144

15-19

487953

gamma-Glutamyltranspeptidase activity and the properties of the extracellular glutaminase from Aspergillus oryzae

1988

Tomita, K.; Ito, M.; Yano, T.; Kumagai, H.; Tochikura, T.

Agric. Biol. Chem.

1159-1163

487956

8095866

Characterization of g-glutamyltranspeptidase from human hepatocellular carcinoma, compared with enzymes from normal liver and cirrhotic liver

1993

Ohta, H.; Sawabu, N.; Kawakami, H.; Watanabe, H.; Ozaki, K.; Toya, D.; Hattori, N.

Clin. Chim. Acta

214

83-92

487961

7816801

Expression of an active glycosylated human gamma-glutamyl transpeptidase mutant that lacks a membrane anchor domain

1995

Ikeda, Y.; Fujii, J.; Taniguchi, N.; Meister, A.

Proc. Natl. Acad. Sci. USA

126-130

487963

8827453

Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase

1996

Ikeda, Y.; Fujii, J.; Taniguchi, N.

J. Biochem.

119

1166-1170

487966

9882013

gamma-Glutamyl transpeptidase-dependent mutagenicity and cytotoxicity of gamma-glutamyl derivatives: a model for biochemical targeting of chemotherapeutic agents

1998

Keren, R.; Stark, A.A.

Environ. Mol. Mutagen.

377-386

487967

10759537

Purified gamma-glutamyl transpeptidases from tomato exhibit high affinity for glutathione and glutathione S-conjugates

2000

Martin, M.N.; Slovin, J.P.

Plant Physiol.

122

1417-1426

487969

11342044

Changes in the kinetic parameters of hepatic gamma-glutamyltransferase from streptozotocin-induced diabetic rats

2001

Cornwell, P.D.; Watkins, J.B.

Biochim. Biophys. Acta

1545

184-191

487972

11891265

gamma-Glutamyl transpeptidase in transgenic tobacco plants. Cellular localization, processing, and biochemical properties

2002

Storozhenko, S.; Belles-Boix, E.; Babiychuk, E.; Herouart, D.; Davey, M.W.; Slooten, L.; Van Montagu, M.; Inze, D.; Kushnir, S.

Plant Physiol.

128

1109-1119

487975

5781001

Isolation and properties of gamma-L-glutamylcyclotransferase from human brain

1969

Orlowski, M.; Richman, P.G.; Meister, A.

Biochemistry

1048-1055

487978

4735346

gamma-Glutamyl cyclotransferase. Distribution, isozymic forms, and specificity

1973

Orlowski, M.; Meister, A.

J. Biol. Chem.

248

2836-2844

487979

gamma-Glutamylcyclotransferase from rat kidney

1981

Meister, A.

Methods Enzymol.

113

428-445

487982

Enzymology of pyrrolidone carboxylic acid

1971

Orlowski, M.; Meister, A.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

123-151

487986

Purification, properties and function of a unique gamma-glutamyl cyclotransferase from the housefly, Musca domestica

1973

Bodnaryk, R.P.; McGirr, L.

Biochim. Biophys. Acta

315

352-362

657592

14602592

Use of bacterial gamma-glutamyltranspeptidase for enzymatic synthesis of gamma-D-glutamyl compounds

2003

Suzuki, H.; Izuka, S.; Minami, H.; Miyakawa, N.; Ishihara, S.; Kumagai, H.

Appl. Environ. Microbiol.

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Links to other databases for 5-L-glutamyl-4-nitroanilide

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ChEBI

PubChem

Ligand 5-L-glutamyl-4-nitroanilide

Basic Ligand Information

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (127 results)

Product in Enzyme-catalyzed Reactions (2 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (37 results)

KM Value (76 results)

References & Links

Literature References (116)

Links to other databases for 5-L-glutamyl-4-nitroanilide

k_cat Value (Turnover Number) (37 results)

K_M Value (76 results)