allantoate amidohydrolase [Pseudoalteromonas sp. 2CM28B]
Protein Classification
Zn-dependent hydrolase( domain architecture ID 11483787)
M20 family Zn-dependent hydrolase similar to allantoate amidohydrolase, which converts allantoate to (S)-ureidoglycolate and ammonia
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| PRK09290 | PRK09290 | allantoate amidohydrolase; Reviewed |
21-419 | 8.25e-170 | |||||||
allantoate amidohydrolase; Reviewed : Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 481.96 E-value: 8.25e-170
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| Name | Accession | Description | Interval | E-value | |||||||
| PRK09290 | PRK09290 | allantoate amidohydrolase; Reviewed |
21-419 | 8.25e-170 | |||||||
allantoate amidohydrolase; Reviewed Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 481.96 E-value: 8.25e-170
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| M20_bAS | cd03884 | M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
39-420 | 1.01e-164 | |||||||
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders. Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 468.54 E-value: 1.01e-164
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| hydantase | TIGR01879 | amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ... |
39-419 | 3.84e-117 | |||||||
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds of compounds containing carbamoyl groups or hydantoin rings. These enzymes are members of the broader family of amidases represented by pfam01546. Pssm-ID: 200138 [Multi-domain] Cd Length: 400 Bit Score: 347.57 E-value: 3.84e-117
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| Peptidase_M20 | pfam01546 | Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
91-420 | 2.14e-39 | |||||||
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases. Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 143.64 E-value: 2.14e-39
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| ArgE | COG0624 | Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
47-419 | 6.50e-11 | |||||||
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 63.75 E-value: 6.50e-11
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| Name | Accession | Description | Interval | E-value | |||||||
| PRK09290 | PRK09290 | allantoate amidohydrolase; Reviewed |
21-419 | 8.25e-170 | |||||||
allantoate amidohydrolase; Reviewed Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 481.96 E-value: 8.25e-170
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| M20_bAS | cd03884 | M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
39-420 | 1.01e-164 | |||||||
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders. Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 468.54 E-value: 1.01e-164
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| PRK12890 | PRK12890 | allantoate amidohydrolase; Reviewed |
21-420 | 5.64e-139 | |||||||
allantoate amidohydrolase; Reviewed Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 403.90 E-value: 5.64e-139
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| PRK12893 | PRK12893 | Zn-dependent hydrolase; |
35-420 | 2.02e-129 | |||||||
Zn-dependent hydrolase; Pssm-ID: 237250 [Multi-domain] Cd Length: 412 Bit Score: 379.22 E-value: 2.02e-129
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| hydantase | TIGR01879 | amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ... |
39-419 | 3.84e-117 | |||||||
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds of compounds containing carbamoyl groups or hydantoin rings. These enzymes are members of the broader family of amidases represented by pfam01546. Pssm-ID: 200138 [Multi-domain] Cd Length: 400 Bit Score: 347.57 E-value: 3.84e-117
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| PRK12892 | PRK12892 | allantoate amidohydrolase; Reviewed |
31-419 | 1.33e-106 | |||||||
allantoate amidohydrolase; Reviewed Pssm-ID: 183817 [Multi-domain] Cd Length: 412 Bit Score: 321.27 E-value: 1.33e-106
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| PRK13590 | PRK13590 | putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional |
38-408 | 3.09e-101 | |||||||
putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional Pssm-ID: 184168 [Multi-domain] Cd Length: 591 Bit Score: 313.23 E-value: 3.09e-101
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| PRK13799 | PRK13799 | unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional |
38-408 | 5.04e-96 | |||||||
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional Pssm-ID: 106740 [Multi-domain] Cd Length: 591 Bit Score: 299.62 E-value: 5.04e-96
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| PRK12891 | PRK12891 | allantoate amidohydrolase; Reviewed |
38-419 | 4.43e-77 | |||||||
allantoate amidohydrolase; Reviewed Pssm-ID: 237249 Cd Length: 414 Bit Score: 245.50 E-value: 4.43e-77
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| Peptidase_M20 | pfam01546 | Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
91-420 | 2.14e-39 | |||||||
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases. Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 143.64 E-value: 2.14e-39
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| M20_Acy1 | cd03886 | M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
226-408 | 3.21e-11 | |||||||
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay. Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 64.54 E-value: 3.21e-11
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| ArgE | COG0624 | Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
47-419 | 6.50e-11 | |||||||
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 63.75 E-value: 6.50e-11
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| PepD2 | COG2195 | Di- or tripeptidase [Amino acid transport and metabolism]; |
47-325 | 7.02e-10 | |||||||
Di- or tripeptidase [Amino acid transport and metabolism]; Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 60.06 E-value: 7.02e-10
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| AbgB | COG1473 | Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
226-408 | 1.64e-08 | |||||||
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 56.28 E-value: 1.64e-08
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| M20_Acy1-like | cd05666 | M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
226-333 | 4.46e-07 | |||||||
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 51.76 E-value: 4.46e-07
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| M20_Acy1_amhX-like | cd08018 | M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
277-356 | 5.37e-06 | |||||||
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 48.05 E-value: 5.37e-06
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| M20_Acy1_YkuR-like | cd05670 | M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
226-333 | 3.76e-05 | |||||||
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs. Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 45.72 E-value: 3.76e-05
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| Peptidase_M28 | pfam04389 | Peptidase family M28; |
75-158 | 9.63e-05 | |||||||
Peptidase family M28; Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 43.04 E-value: 9.63e-05
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| M20_Acy1-like | cd08019 | M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
206-424 | 1.44e-04 | |||||||
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 43.86 E-value: 1.44e-04
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| M28 | cd02690 | M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ... |
75-158 | 1.64e-04 | |||||||
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases. Pssm-ID: 349868 [Multi-domain] Cd Length: 202 Bit Score: 42.72 E-value: 1.64e-04
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| Zinc_peptidase_like | cd03873 | Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
75-169 | 3.47e-04 | |||||||
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues). Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 41.64 E-value: 3.47e-04
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| M20_18_42 | cd18669 | M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
75-164 | 4.44e-04 | |||||||
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues). Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 41.26 E-value: 4.44e-04
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| M28_like | cd05640 | M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ... |
66-158 | 5.61e-04 | |||||||
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. Pssm-ID: 349893 [Multi-domain] Cd Length: 281 Bit Score: 41.66 E-value: 5.61e-04
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| PRK04443 | PRK04443 | [LysW]-lysine hydrolase; |
46-100 | 7.38e-04 | |||||||
[LysW]-lysine hydrolase; Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 41.48 E-value: 7.38e-04
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| M20_CPDG2 | cd03885 | M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
221-323 | 1.57e-03 | |||||||
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells. Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 40.27 E-value: 1.57e-03
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