DB code: D00189

RLCP classification	1.13.30000.10 : Hydrolysis
CATH domain	3.40.50.1820 : Rossmann fold	Catalytic domain
CATH domain	1.10.287.410 : Helix Hairpins
E.C.	3.4.16.5
CSA	1ysc
M-CSA	1ysc
MACiE

CATH domain	Related DB codes (homologues)
3.40.50.1820 : Rossmann fold	S00544 S00344 S00517 S00525 S00526 S00720 S00723 S00724 S00725 S00919 S00057 S00374 S00345 S00347 S00348 S00346 S00350 S00352 S00353 S00355 S00356 S00358 D00210 D00539 T00253

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	RefSeq	MEROPS	Pfam
P00729	Carboxypeptidase Y	EC 3.4.16.5 Carboxypeptidase YSCY	NP_014026.1 (Protein) NM_001182806.1 (DNA/RNA sequence)	S10.001 (Serine)	PF05388 (Carbpep_Y_N) PF00450 (Peptidase_S10) [Graphical View]

KEGG enzyme name
carboxypeptidase C carboxypeptidase Y serine carboxypeptidase I cathepsin A lysosomal protective protein deamidase lysosomal carboxypeptidase A phaseolin

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
P00729	CBPY_YEAST	Release of a C-terminal amino acid with broad specificity.		Vacuole. Note=Lysosome-like vacuoles.

KEGG Pathways
Map code	Pathways	E.C.

Compound table
	Substrates		Products	Intermediates
KEGG-id	C00012	C00001	C00012	I00087	I00085	I00086
E.C.
Compound	Peptide	H2O	Peptide	Peptidyl-tetrahedral intermediate	Acyl-enzyme	Tetrahedral intermediate
Type	peptide/protein	H2O	peptide/protein
ChEBI		15377 15377
PubChem		22247451 962 22247451 962

1cpyA01	Unbound		Unbound
1yscA01	Unbound		Unbound
1cpyA02	Unbound		Unbound
1yscA02	Unbound		Unbound

Reference for Active-site residues
resource	references	E.C.

Active-site residues
PDB	Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment

1cpyA01	SER 146;ASP 338;HIS 397
1yscA01	SER 146;ASP 338;HIS 397
1cpyA02
1yscA02

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis
[2]	p.11116
[4]	Fig.8

References
[1]
Resource
Comments
Medline ID
PubMed ID	1459131
Journal	Eur J Biochem
Year	1992
Volume	210
Pages	467-73
Authors	Christensen U, Drohse HB, Molgaard L
Title	Mechanism of carboxypeptidase-Y-catalysed peptide semisynthesis.
Related PDB
Related UniProtKB
[2]
Resource
Comments	X-ray crystallography (2.8 Angstroms)
Medline ID
PubMed ID	7727362
Journal	Biochemistry
Year	1994
Volume	33
Pages	11106-20
Authors	Endrizzi JA, Breddam K, Remington SJ
Title	2.8-A structure of yeast serine carboxypeptidase.
Related PDB	1cpy 1ysc
Related UniProtKB	P00729
[3]
Resource
Comments	catalysis
Medline ID
PubMed ID
Journal	J Am Chem Soc
Year	1995
Volume	117
Pages	5944
Authors	Sorensen SB, Raaschou-Nielsen M, Mortensen UH, Remington SJ, Breddam K
Title	Site-directed mutagenesis on (serine) carboxypeptidase y from yeast. The significance of thr 60 and met 398 in hydrolysis and aminolysis reactions.
Related PDB	1cpy
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID	8679540
Journal	Biochemistry
Year	1996
Volume	35
Pages	7131-41
Authors	Stennicke HR, Mortensen UH, Breddam K
Title	Studies on the hydrolytic properties of (serine) carboxypeptidase Y.
Related PDB
Related UniProtKB
[5]
Resource
Comments	catalysis (ligand specificity)
Medline ID
PubMed ID	9336845
Journal	Protein Sci
Year	1997
Volume	6
Pages	2227-32
Authors	Sorensen SB, Breddam K
Title	The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocket.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID	10021925
Journal	Bioorg Med Chem Lett
Year	1999
Volume	9
Pages	187-92
Authors	Mock WL, Xu D
Title	Catalytic activity of carboxypeptidase B and of carboxypeptidase Y with anisylazoformyl substrates.
Related PDB
Related UniProtKB
[7]
Resource
Comments	conformational stability
Medline ID
PubMed ID	10336632
Journal	Eur J Biochem
Year	1999
Volume	262
Pages	475-83
Authors	Dumoulin M, Ueno H, Hayashi R, Balny C
Title	Contribution of the carbohydrate moiety to conformational stability of the carboxypeptidase Y high pressure study.
Related PDB
Related UniProtKB
[8]
Resource
Comments	catalysis (mutation analysis)
Medline ID
PubMed ID	10427689
Journal	Biosci Biotechnol Biochem
Year	1999
Volume	63
Pages	1045-50
Authors	Shimizu H, Ueno H, Hayashi R
Title	Role of carbohydrate moiety in carboxypeptidase Y: structural study of mutant enzyme lacking carbohydrate moiety.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the peptidase family S10. According to the literature [2], this enzyme contains a catalytic triad, Ser146/Asp338/His397 (PDB; 1cpy), which is similar to those of trypsine-like serine peptidases. In this enzyme, Ser146 acts as a nucleophile, and His397 acts as Acid/Base. The negatively charged tetrahedral intermediate during catalysis is stablized by the oxyanion hole composed of the backbone amides.

Comments

This enzyme belongs to the peptidase family S10.
According to the literature [2], this enzyme contains a catalytic triad, Ser146/Asp338/His397 (PDB; 1cpy), which is similar to those of trypsine-like serine peptidases. In this enzyme, Ser146 acts as a nucleophile, and His397 acts as Acid/Base. The negatively charged tetrahedral intermediate during catalysis is stablized by the oxyanion hole composed of the backbone amides.

Created	Updated
2003-01-27	2011-02-16