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Information on EC 3.5.2.2 - dihydropyrimidinase and Organism(s) Paenarthrobacter aurescens and UniProt Accession P81006

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.2 In cyclic amides
                3.5.2.2 dihydropyrimidinase
IUBMB Comments
Also acts on dihydrothymine and hydantoin.
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This record set is specific for:
Paenarthrobacter aurescens
UNIPROT: P81006
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The taxonomic range for the selected organisms is: Paenarthrobacter aurescens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
dhp, dihydropyrimidine dehydrogenase, dihydropyrimidinase, hydantoinase, d-hydantoinase, dhp-1, dhpase, dihydropyrimidine amidohydrolase, dhp-2, padhpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-hydantoinase
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DHP
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Dihydropyrimidinase
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hydantoin peptidase
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hydantoinase
hydropyrimidine hydrase
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pyrimidine hydrase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
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SYSTEMATIC NAME
IUBMB Comments
5,6-dihydropyrimidine amidohydrolase
Also acts on dihydrothymine and hydantoin.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-74-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,6-dihydrouracil + H2O
3-ureidopropionate
show the reaction diagram
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-
-
-
?
dihydrothymidine + H2O
?
show the reaction diagram
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-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
show the reaction diagram
-
-
-
-
?
DL-5-indolylmethylhydantoin + H2O
L-tryptophan
show the reaction diagram
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
show the reaction diagram
-
-
-
-
?
DL-fluorobromylhydantoin + H2O
?
show the reaction diagram
-
-
-
-
?
DL-methylthioethylhydantoin + H2O
?
show the reaction diagram
-
D-selective for the hydrolysis
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-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5,6-dihydrouracil + H2O
3-ureidopropionate
show the reaction diagram
-
-
-
-
?
dihydrothymidine + H2O
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
a binuclear zinc center activates a water molecule for nucleophilic attack on the substrates‘ amide bond
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
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10 mM dihydrouracil as substrate
0.3
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DL-phenylhydantoin, 50 mM
0.4
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10 mM dihydrothymine as substrate
0.6
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DL-methylhydantoin, 57 mM
1.5
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L-methylthioethylhydantoin, 2 mM
12
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L-methylthioethylhydantoin, 20 mM
13
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DL-5-indolylmethylhydantoin as substrate
30
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DL-methylthioethylhydantoin, 40 mM
37
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D-methylthioethylhydantoin, 20 mM
5.4
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D-methylthioethylhydantoin, 2 mM
70
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L-5-indolylmethylhydantoin as substrate
76.6
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DL-fluorobromylhydantoin as substrate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HYDL_PAEAU
458
0
49597
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
-
native enzyme
247000
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calculated according to the repective amount of Zn2+
49680
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MALDI-MS studies, single charged monomer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
each subunit of the tetrameric enzyme consists of an elliptically distorted (alpha/beta)8-barrel domain
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.6 A resolution. Crystals belong to the space group p2(1) with unit cell parameters a = 111.55 A, b = 74.28 A, c = 146.87 A and beta = 106.7 A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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production of enantiomeric pure nonproteinogenic amino acids, currently under investigation in bioprocess scale for industrial application
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
May, O.; Siemann, M.; Pietzsch, M.; Kiess, M.; Mattes, R.; Syldatk, C.
Substrate-dependent enantioselectivity of a novel hydantoinase from Arthrobacter aurescens DSM 3745: Purification and characterization as new member of cyclic amidases
J. Biotechnol.
61
1-13
1998
Agrobacterium tumefaciens, Paenarthrobacter aurescens, Arthrobacter sp., Geobacillus stearothermophilus, Brevibacillus brevis, Bos taurus, Flavobacterium sp., Pseudomonas putida, Pseudomonas stutzeri, Rattus norvegicus, Geobacillus stearothermophilus JC2310, Arthrobacter sp. DSM 3747
Manually annotated by BRENDA team
Siemann, M.; Alvarado-Marin, A.; Pietzsch, M.; Syldatk, C.
A D-specific hydantoin amidohydrolase: properties of the metalloenzyme purified from Arthrobacter crystallopoietes
J. Mol. Catal. , B Enzym.
6
387-397
1999
Agrobacterium tumefaciens, Agrobacterium sp., Paenarthrobacter aurescens, Arthrobacter crystallopoietes, Geobacillus stearothermophilus, Bacillus sp. (in: Bacteria), Parageobacillus thermoglucosidasius, Homo sapiens, Pseudomonas sp., Pseudomonas putida, Pseudomonas fluorescens, Rattus norvegicus, Agrobacterium sp. IP-I 671, Pseudomonas sp. AJ-11220, Bacillus sp. (in: Bacteria) LU 1220
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Manually annotated by BRENDA team
Abendroth, J.; Niefind, K.; May, O.; Siemann, M.; Syldatk, C.; Schomburg, D.
The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity
Biochemistry
41
8589-8597
2002
Paenarthrobacter aurescens (P81006), Paenarthrobacter aurescens
Manually annotated by BRENDA team
Suzuki, S.; Takenaka, Y.; Onishi, N.; Yokozeki, K.
Molecular cloning and expression of the hyu genes from Microbacterium liquefaciens AJ 3912, responsible for the conversion of 5-substituted hydantoins to alpha-amino acids, in Escherichia coli
Biosci. Biotechnol. Biochem.
69
1473-1482
2005
Microbacterium liquefaciens, Paenarthrobacter aurescens (P81006), Microbacterium liquefaciens AJ3912
Manually annotated by BRENDA team
Radha Kishan, K.V.; Vohra, R.M.; Ganesan, K.; Agrawal, V.; Sharma, V.M.; Sharma, R.
Molecular structure of D-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition
J. Mol. Biol.
347
95-105
2005
Paenarthrobacter aurescens, Geobacillus stearothermophilus, Bacillus sp. (in: Bacteria), Ralstonia pickettii, Thermus sp., Bacillus sp. (in: Bacteria) AR9
Manually annotated by BRENDA team