L-hydantoinase
Details
- Name
- L-hydantoinase
- Kind
- protein
- Synonyms
- 3.5.2.-
- Non-ATP-dependent L-selective hydantoinase
- Gene Name
- lhyD
- UniProtKB Entry
- P81006Swiss-Prot
- Organism
- Arthrobacter aurescens
- NCBI Taxonomy ID
- 43663
- Amino acid sequence
>lcl|BSEQ0011268|L-hydantoinase MFDVIVKNCRLVSSDGITEADILVKDGKVAAISADTSDVEASRTIDAGGKFVMPGVVDEH VHIIDMDLKNRYGRFELDSESAAVGGITTIIEMPITFPPTTTLDAFLEKKKQAGQRLKVD FALYGGGVPGNLPEIRKMHDAGAVGFKSMMAASVPGMFDAVSDGELFEIFQEIAACGSVI VVHAENETIIQALQKQIKAAGGKDMAAYEASQPVFQENEAIQRALLLQKEAGCRLIVLHV SNPDGVELIHQAQSEGQDVHCESGPQYLNITTDDAERIGPYMKVAPPVRSAEMNIRLWEQ LENGLIDTLGSDHGGHPVEDKEPGWKDVWKAGNGALGLETSLPMMLTNGVNKGRLSLERL VEVMCEKPAKLFGIYPQKGTLQVGSDADLLILDLDIDTKVDASQFRSLHKYSPFDGMPVT GAPVLTMVRGTVVAEKGEVLVEQGFGQFVTRRNYEASK
- Number of residues
- 458
- Molecular Weight
- 49596.275
- Theoretical pI
- 4.66
- GO Classification
- Functionsallantoinase activity / cobalt ion binding / zinc ion bindingProcessesallantoin catabolic process
- General Function
- Rather more predominant for the cleavage of aryl- than for alkyl-hydantoin derivatives. The stereoselectivity of this enzyme depends on the substrate used for bioconversion: strictly L-selective for the cleavage of D,L-5-indolylmethylhydantoin, but D-selective for the hydrolysis of D,L-methylthioethylhydantoin.
- Specific Function
- allantoinase activity
- Pfam Domain Function
- Amidohydro_1 (PF01979)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
- Not Available
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P81006 UniProtKB Entry Name HYDL_ARTAU PDB ID(s) 1GKR - General References
- May O, Habenicht A, Mattes R, Syldatk C, Siemann M: Molecular evolution of hydantoinases. Biol Chem. 1998 Jun;379(6):743-7. [Article]
- 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. 1998 Mar 26;61(1):1-13. [Article]
- May O, Siemann M, Syldatk C, Niefind K, Schomburg D: Crystallization and preliminary X-ray analysis of a hydantoinase from Arthrobacter aurescens DSM 3745. Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1209-10. [Article]
- 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. 2002 Jul 9;41(27):8589-97. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Lysine Nz-Carboxylic Acid experimental unknown target Details