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Information on EC 3.6.1.60 - diadenosine hexaphosphate hydrolase (AMP-forming)
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3.6.1.60 diadenosine hexaphosphate hydrolase (AMP-forming)IUBMB Comments
A divalent cation is essential for activity. Mn2+ (2--6 mM) is most effective.
The enzyme controls intracellular levels of P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate. Weak activity with P1,P4-bis(5'-adenosyl)tetraphosphate. Marked preference for adenine over guanine nucleotides.
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Word Map
- 3.6.1.60
- polyphosphates
-
diphosphoinositol
- prostate
- autoantibody
-
nudix
-
serous
-
nappa
-
tumor-associated
- dipps
-
phosphohydrolases
- trim39
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
nudt10, nudt11, haps1, haps2, atnudt13, at3g26690, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP
(2)
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP
(2)
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP
-
-
-
-
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-pentaphosphate + AMP
(1)
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-pentaphosphate + AMP
-
-
-
-
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-tetraphosphate + ADP
(1)
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-tetraphosphate + ADP
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (AMP-forming)
A divalent cation is essential for activity. Mn2+ (2--6 mM) is most effective.
The enzyme controls intracellular levels of P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate. Weak activity with P1,P4-bis(5'-adenosyl)tetraphosphate. Marked preference for adenine over guanine nucleotides.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
ATP + AMP
weak activity
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
P1,P5-bis(5'-adenosyl)pentaphosphate is hydrolyzed at 40% of the activity compared to P1,P6-bis(5'-adenosyl)hexaphosphate
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
marked preference for adenine over guanine nucleotides. The enzyme controls intracellular P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate levels
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
marked preference for adenine over guanine nucleotides. The most rapidly metabolised substrate appears to be P1,P5-bis(5'-adenosyl)pentaphosphate, although P1,P6-bis(5'-adenosyl)hexaphosphate is bound with higher affinity
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
the enzyme degrades P1,P6-bis(5'-adenosyl)hexaphosphate and P1,P5-bis(5'-adenosyl)pentaphosphate, in preference to other diadenosine polyphosphates
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
the function of the enzyme may be to eliminate potentially toxic dinucleoside polyphosphates during sporulation
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
hydrolysis of P1,P5-bis(5'-adenosyl)pentaphosphate yields predominantly AMP and adenosine tetraphosphate (96%)
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
marked preference for adenine over guanine nucleotides. The enzyme controls intracellular P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate levels
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
marked preference for adenine over guanine nucleotides. The most rapidly metabolised substrate appears to be P1,P5-bis(5'-adenosyl)pentaphosphate, although P1,P6-bis(5'-adenosyl)hexaphosphate is bound with higher affinity
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
the predominant route of P1,P6-bis(5'-adenosyl)hexaphosphate hydrolysis is to AMP plus P1,P5-bis(5'-adenosyl)pentaphosphate, with the formation of ADP plus p4A being a more minor reaction. The enzyme degrades P1,P6-bis(5'-adenosyl)hexaphosphate and P1,P5-bis(5'-adenosyl)pentaphosphate, in preference to other diadenosine polyphosphates
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
-
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
preferred substrate. Hydrolysis of P1,P6-bis(5'-adenosyl)hexaphosphate with the formation of ADP or AMP
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
the function of the enzyme may be to eliminate potentially toxic dinucleoside polyphosphates during sporulation
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
hydrolysis in H218O shows that ADP and adenosine 5*-tetraphosphate are produced by attack at Pbeta and AMP and adenosine 5'-pentaphosphate are produced by attack at Palpha (76%) and AMP and adenosine 5'-pentaphosphate are produced by attack at Palpha (24%). P1,P6-bis(5'-adenosyl)hexaphosphate is a 8fold better substrate than P1,P5-bis(5'-adenosyl)pentaphosphate
-
-
?
additional information
?
-
diadenosine tetraphosphate and diadenosine triphosphate, adenosine nucleotides, diphosphoinositol polyphosphate and phosphoribosyl pyrophosphate are not hydrolyzed
-
-
?
additional information
?
-
-
diadenosine tetraphosphate and diadenosine triphosphate, adenosine nucleotides, diphosphoinositol polyphosphate and phosphoribosyl pyrophosphate are not hydrolyzed
-
-
?
additional information
?
-
the enzyme also catalyses the hydrolysis of diphosphoinositol pentakisphosphate
-
-
?
additional information
?
-
no activity with P1,P4-bis(5'-adenosyl)tetraphosphate or other dinucleotides, mononucleotides, nucleotide sugars, or nucleotide alcohols
-
-
?
additional information
?
-
endopolyphosphatase activity is analyzed by the decrease in polyphosphate chain length (polyphosphate208 and polyphosphate15)
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
marked preference for adenine over guanine nucleotides. The enzyme controls intracellular P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate levels
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
marked preference for adenine over guanine nucleotides. The enzyme controls intracellular P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate levels
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
the function of the enzyme may be to eliminate potentially toxic dinucleoside polyphosphates during sporulation
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
-
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
the function of the enzyme may be to eliminate potentially toxic dinucleoside polyphosphates during sporulation
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
Cu2+
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
Mg2+
Mn2+
Zn2+
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
additional information
Mn2+
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
additional information
Mg2+, Ni2+ and Ca1+ are not able to activate the enzyme
additional information
Mg2+, Ni2+ and Ca1+ are not able to activate the enzyme
additional information
-
Mg2+, Ni2+ and Ca1+ are not able to activate the enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
inhibits the endopolyphophatase of the recombinant enzyme DDP1
diphosphate
inhibits the endopolyphophatase of the recombinant enzyme DDP1
phosphate
inhibits the endopolyphophatase of the recombinant enzyme DDP1
Triphosphate
inhibits the endopolyphophatase of the recombinant enzyme DDP1
additional information
ADP has no effect on the endopolyphophatase activity of recombinant DDP1
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
the enzyme requires reducing conditions for optimal activity. The omission of dithiothreitol from the enzymatic reactions reduces its activity by 70%
dithiothreitol
absolute requirement for a reducing agent, such as dithiothreitol (1 mM)
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Asthma
Suggestive association between variants in IL1RAPL and asthma symptoms in Latin American children.
Neoplasms
Bioinformatics Analysis Reveals an Association Between Cancer Cell Stemness, Gene Mutations, and the Immune Microenvironment in Stomach Adenocarcinoma.
Neoplasms
Exploring targets of TET2-mediated methylation reprogramming as potential discriminators of prostate cancer progression.
Ovarian Neoplasms
Systematic review: Tumor-associated antigen autoantibodies and ovarian cancer early detection.
Ovarian Neoplasms
Tumor-associated autoantibodies as early detection markers for ovarian cancer? A prospective evaluation.
Prostatic Neoplasms
Genetic and functional analyses implicate the NUDT11, HNF1B, and SLC22A3 genes in prostate cancer pathogenesis.
Prostatic Neoplasms
NUDT11 rs5945572 polymorphism and prostate cancer risk: a meta-analysis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 7.6, 37°C, hApsI-39N
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9
7.5 - 9
pH 7.5: about 55% of maximal activity, pH 8.5-9: maximal activity
7.5 - 9
pH 7.5: about 60% of maximal activity, pH 9: about 90% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
no signal for hAps1 is detected in placenta, liver, skeletal muscle, kidney, spleen, colon or peripheral blood leukocytes. No activity in breast GI-101 cells, lung LX-1 cells, colon CX-1 cells, lung GI-117 cells, colon GI-112 cells and pancreas GI-103 cells
brenda
additional information
no signal for hAps1 is detected in placenta, liver, skeletal muscle, kidney, spleen, colon or peripheral blood leukocytes. No activity in breast GI-101 cells, lung LX-1 cells, colon CX-1 cells, lung GI-117 cells, colon GI-112 cells and pancreas GI-103 cells
brenda
additional information
-
no signal for hAps1 is detected in placenta, liver, skeletal muscle, kidney, spleen, colon or peripheral blood leukocytes. No activity in breast GI-101 cells, lung LX-1 cells, colon CX-1 cells, lung GI-117 cells, colon GI-112 cells and pancreas GI-103 cells
brenda
additional information
no signal for hAps2 is found in skeletal muscle, thymus, small intestine, colon or peripheral blood leukocytes. No activity in tumour cell lines from breast GI-101, lung LX-1, colon CX-1, lung GI-117, colon GI-112 and pancreas GI-103
brenda
additional information
no signal for hAps2 is found in skeletal muscle, thymus, small intestine, colon or peripheral blood leukocytes. No activity in tumour cell lines from breast GI-101, lung LX-1, colon CX-1, lung GI-117, colon GI-112 and pancreas GI-103
brenda
additional information
-
no signal for hAps2 is found in skeletal muscle, thymus, small intestine, colon or peripheral blood leukocytes. No activity in tumour cell lines from breast GI-101, lung LX-1, colon CX-1, lung GI-117, colon GI-112 and pancreas GI-103
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively. The average chain length of salt-soluble and alkali-soluble fractions does not change in the overexpressing strain, and that of acid-soluble polyphosphate increases under phosphate excess. At the initial stage of polyphosphate recovery after phosphorus starvation, the chain length of the acid-soluble fraction in transformed cells is lower compared to the recipient strain. In DDP1 deletion mutant, the level of inositol pyrophosphate is twice higher, while the level of polyphosphate is reduced. The overexpression of DDP1 probably leads to a decrease in the level of diphosphoinositol pentakisphosphate and bis(diphosphoinositol) tetrakisphosphate in the cell. These compounds seem to be involved in the regulation of polyphosphate synthesis and degradation
metabolism
diphosphoinositol polyphosphate phosphohydrolase (DDP1, EC 3.6.1.52) is also a diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60) and shows endopolyphosphatase (EC 3.6.1.10) activity. The relationship between inositol pyrophosphate and polyphosphate metabolisms seems to be complicated
physiological function
yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) having endopolyphosphatase activity on inorganic polyphosphate metabolism in Saccharomyces cerevisiae. Complex nature of DDP1 involvement in the regulation of polyphosphate content and chain length in yeasts
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DDP1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
188
0
21572
Swiss-Prot
other Location (Reliability: 2)
NUD10_HUMAN
164
0
18500
Swiss-Prot
other Location (Reliability: 2)
NUD10_MOUSE
164
0
18593
Swiss-Prot
other Location (Reliability: 2)
NUD11_BOVIN
164
0
18519
Swiss-Prot
other Location (Reliability: 3)
NUD11_HUMAN
164
0
18559
Swiss-Prot
other Location (Reliability: 3)
NUD11_MOUSE
164
0
18593
Swiss-Prot
other Location (Reliability: 2)
A0A2P6SA28_ROSCH
174
0
19577
TrEMBL
Mitochondrion (Reliability: 3)
A0A072VMC0_MEDTR
66
0
7431
TrEMBL
other Location (Reliability: 5)
A0A3G2S8Y8_9BASI
170
0
19559
TrEMBL
other Location (Reliability: 2)
A0A2P6QZY3_ROSCH
214
0
24131
TrEMBL
Mitochondrion (Reliability: 2)
A0A2P6S6P9_ROSCH
262
0
30080
TrEMBL
Chloroplast (Reliability: 2)
A0A072U2X6_MEDTR
221
0
25673
TrEMBL
Mitochondrion (Reliability: 4)
G7LGT1_MEDTR
175
0
20167
TrEMBL
Mitochondrion (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
overexpression of yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) in Saccharomyces cerevisiae leads to significantly increased compared to the parent strain. The content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively
additional information
-
overexpression of yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) in Saccharomyces cerevisiae leads to significantly increased compared to the parent strain. The content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene DDP1, recombinant overexpression in Saccharomyces cerevisiae strain CRN. The initial strain CRN lacks the endopolyphosphatase PPN1, but has its own protein DDP1, which accounts for the low endopolyphosphatase activity in this strain. The recombinant DDP1 enzyme shows an endopolyphosphatase activity, the endopolyphosphatase activity of the transformant manifests itself both with long-chain polyP208 and with short-chain polyP15. Content of phosphate and polyphosphate in cells of CRN, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
suppressing the expression of NUDT11, SLC22A3, and HNF1B influences cellular phenotypes associated with tumor-related properties in prostate cancer cells. 4 of the 12 known risk polymorphisms are strongly associated with transcripts NUDT11, MSMB, NCOA4, SLC22A3, and HNF1B in histologically normal tissue. Although associations are also observed in tumor tissue, they tend to be more attenuated
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Safrany, S.T.; Ingram, S.W.; Cartwright, J.L.; Falck, J.R.; McLennan, A.G.; Barnes, L.D.; Shears, S.B.
The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein
J. Biol. Chem.
274
21735-21740
1999
Homo sapiens (O95989)
brenda
Leslie, N.R.; McLennan, A.G.; Safrany, S.T.
Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases
BMC Biochem.
3
20
2002
Homo sapiens (Q8NFP7), Homo sapiens (Q96G61), Homo sapiens
brenda
Olejnik, K.; Murcha, M.W.; Whelan, J.; Kraszewska, E.
Cloning and characterization of AtNUDT13, a novel mitochondrial Arabidopsis thaliana Nudix hydrolase specific for long-chain diadenosine polyphosphates
FEBS J.
274
4877-4885
2007
Arabidopsis thaliana (Q52K88), Arabidopsis thaliana
brenda
Cartwright, J.L.; McLennan, A.G.
The Saccharomyces cerevisiae YOR163w gene encodes a diadenosine 5', 5"'-P1,P6-hexaphosphate (Ap6A) hydrolase member of the MutT motif (Nudix hydrolase) family
J. Biol. Chem.
274
8604-8610
1999
Saccharomyces cerevisiae (Q99321)
brenda
Grisanzio, C.; Werner, L.; Takeda, D.; Awoyemi, B.C.; Pomerantz, M.M.; Yamada, H.; Sooriakumaran, P.; Robinson, B.D.; Leung, R.; Schinzel, A.C.; Mills, I.; Ross-Adams, H.; Neal, D.E.; Kido, M.; Yamamoto, T.; Petrozziello, G.; Stack, E.C.; Lis, R.; Kantoff, P.W.; Loda, M.; Sartor, O.; Egawa, S.; Tewari, A.K.
Genetic and functional analyses implicate the NUDT11, HNF1B, and SLC22A3 genes in prostate cancer pathogenesis
Proc. Natl. Acad. Sci. USA
109
11252-11257
2012
Homo sapiens (Q96G61), Homo sapiens
brenda
Trilisenko, L.V.; Andreeva, N.A.; Eldarov, M.A.; Dumina, M.V.; Kulakovskaya, T.V.
Polyphosphates and polyphosphatase activity in the yeast Saccharomyces cerevisiae during overexpression of the DDP1 gene
Biochemistry
80
1312-1317
2015
Saccharomyces cerevisiae (Q99321), Saccharomyces cerevisiae ATCC 204508 (Q99321)
brenda
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