Literature summary for 4.3.1.17 extracted from

Yamada, T.; Komoto, J.; Kasuya, T.; Takata, Y.; Ogawa, H.; Mori, H.; Takusagawa, F.
A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies (2008), Biochim. Biophys. Acta, 1780, 809-818.

Search for more literature for 4.3.1.17

Cloned(Commentary)

Cloned (Comment)	Organism
cancer cell isozyme cSDH, expression in Escherichia coli strain BL21	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant cSDH, hanging drop vapour diffusion method, 10 mg/ml protien in 50 mM Na-citrate, pH 5.6, 10 mM DL-O-methylserine, 200 mM potassium acetate, 5 mM dithiothreitol, 15% w/v PEG-8000 at 21°C, 1 week, X-ray diffraction structure determination and analysis at 2.8 A resolution	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
A65G	site-directed mutagenesis of the human liver isozyme cSDH, large structural alterations, serine binding is not affected, overview	Homo sapiens
C303A	site-directed mutagenesis of the human liver isozyme cSDH, structural alterations, overview	Homo sapiens
C309A	site-directed mutagenesis of the cancer cell isozyme cSDH, structural alterations, overview	Homo sapiens
G72A	site-directed mutagenesis of the cancer cell isozyme cSDH, large structural alterations, serine binding is not affected, changing alanine to glycine at residue 72 in cSDH is responsible for the reduced catalytic activity of cSDH, overview	Homo sapiens
G72A/S228A	site-directed mutagenesis of the cancer cell isozyme cSDH, catalytic activities for both the substrates are substantially recovered, overview	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-serine	Homo sapiens	SDH is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes dehydration of L-Ser/Thr to yield pyruvate/ketobutyrate and ammonia	pyruvate + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q96GA7	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant cancer cell isozyme cSDH to homogeneity by ammonium sulfate fractionation, dialysis, anion exchange and nickel affinity chromatography	Homo sapiens

Reaction

Reaction	Comment	Organism	Reaction ID
L-serine = pyruvate + NH3	catalytic mechanism	Homo sapiens	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
carcinoma cell line	cancer cell line-specific isozyme cSDH	Homo sapiens	-
liver	hSDH, mainly	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-serine	SDH is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes dehydration of L-Ser/Thr to yield pyruvate/ketobutyrate and ammonia	Homo sapiens	pyruvate + NH3	-	?
L-serine	a rigid pyridine ring pocket is necessary for cSDH having a flexible substrate binding-loop	Homo sapiens	pyruvate + NH3	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Homo sapiens
More	structure analysis and comparison to the rat and the human liver isozymes, the cancer cell isozyme and the liver isozyme show different active site surface amino acid residues, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
SDH	-	Homo sapiens
SDH-like-1	-	Homo sapiens
serine dehydratase like-1	-	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.3	-	assay at	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	SDH is a pyridoxal 5'-phosphate-dependent enzyme, PLP is covalently attached to K48 by Schiff-base linkage in the active site. The ring nitrogen of PLP is involved in a H-bonding with C309, but is apparently not protonated	Homo sapiens

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Release 2023.1 (January 2023)