Abstract
The results of studies on the substrate specificities of elimination and replacement reactions allowed insight into the active and regulatory sites of Streptomyces phaeochromogenes cystathionine γ-lyase l-cystathionine cysteine-lyase (deaminating), EC 4.4.1.1). The enzyme has an active site and a regulatory site. The active site consists of two subsites; one recognizes the l-forms of animo acids (l-homoserine and l-moieties of cystathionine isomers) and the other shows affinity for thiol compounds with a carboxyl group. The regulatory site is specific for l-cysteine and has no affinity for ordinary thiol compounds, such as 3-mercaptopropionate and thioglycolate.
| Original language | English |
|---|---|
| Pages (from-to) | 45-50 |
| Number of pages | 6 |
| Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
| Volume | 913 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - May 27 1987 |
| Externally published | Yes |
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Keywords
- (S. phaeochromogenes)
- Cystathionine γ-lyase
- Elimination reaction
- Pyridoxal phosphate enzyme
- Replacement reaction
- Substrate specificity
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
- Structural Biology
Cite this
Insight into the active site of Streptomyces cystathionine γ-lyase based on the results of studies on its substrate specificity. / Kanzaki, Hiroshi; Nagasawa, Toru; Yamada, Hideaki.
In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 913, No. 1, 27.05.1987, p. 45-50.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Insight into the active site of Streptomyces cystathionine γ-lyase based on the results of studies on its substrate specificity
AU - Kanzaki, Hiroshi
AU - Nagasawa, Toru
AU - Yamada, Hideaki
PY - 1987/5/27
Y1 - 1987/5/27
N2 - The results of studies on the substrate specificities of elimination and replacement reactions allowed insight into the active and regulatory sites of Streptomyces phaeochromogenes cystathionine γ-lyase l-cystathionine cysteine-lyase (deaminating), EC 4.4.1.1). The enzyme has an active site and a regulatory site. The active site consists of two subsites; one recognizes the l-forms of animo acids (l-homoserine and l-moieties of cystathionine isomers) and the other shows affinity for thiol compounds with a carboxyl group. The regulatory site is specific for l-cysteine and has no affinity for ordinary thiol compounds, such as 3-mercaptopropionate and thioglycolate.
AB - The results of studies on the substrate specificities of elimination and replacement reactions allowed insight into the active and regulatory sites of Streptomyces phaeochromogenes cystathionine γ-lyase l-cystathionine cysteine-lyase (deaminating), EC 4.4.1.1). The enzyme has an active site and a regulatory site. The active site consists of two subsites; one recognizes the l-forms of animo acids (l-homoserine and l-moieties of cystathionine isomers) and the other shows affinity for thiol compounds with a carboxyl group. The regulatory site is specific for l-cysteine and has no affinity for ordinary thiol compounds, such as 3-mercaptopropionate and thioglycolate.
KW - (S. phaeochromogenes)
KW - Cystathionine γ-lyase
KW - Elimination reaction
KW - Pyridoxal phosphate enzyme
KW - Replacement reaction
KW - Substrate specificity
UR - http://www.scopus.com/inward/record.url?scp=0023217706&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023217706&partnerID=8YFLogxK
U2 - 10.1016/0167-4838(87)90230-5
DO - 10.1016/0167-4838(87)90230-5
M3 - Article
C2 - 3580375
AN - SCOPUS:0023217706
VL - 913
SP - 45
EP - 50
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
SN - 1570-9639
IS - 1
ER -