BRENDA home
History
Information on EC 1.1.1.299 - malate dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.299Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.299 malate dehydrogenase [NAD(P)+]IUBMB Comments
This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity .
Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 (malate dehydrogenase (quinone)).
Specify your search results
Word Map
- 1.1.1.299
- maldhs
-
nad-dependent
- dehydrogenases
- l-lactate
- l-malate
-
hyperthermophilic
-
archaeon
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
LDH-like MalDH, MDH II, NAD(P)-dependent malate dehydrogenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
-
-
-
-
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
ordered bi-bi mechanism
-
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
ordered bi-bi mechanism
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NAD(P)+ oxidoreductase
This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity [1].
Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 (malate dehydrogenase (quinone)).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9001-64-3
cf. EC 1.1.1.37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
the enzyme strongly prefers oxaloacetate by three orders of magnitude compared to pyruvate
-
-
?
additional information
?
-
-
enzyme shows pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of the coenzyme. No substrates are: D-malate, malonate, L-glutamate, L-aspartate, D,L-2-hydroxybutanoate, D,L-3-hydroxybutanoate, citrate, maleate, succinate, L-tartrate, L-threonine, L-serine, L-hydroxymalonate, D-glutamate, 2-oxocaproate, 2-oxoisovalerate, glyoxylate, 2-oxoglutarate, 2-oxobutanoate
-
-
?
additional information
?
-
-
enzyme shows pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of the coenzyme. No substrates are: D-malate, malonate, L-glutamate, L-aspartate, D,L-2-hydroxybutanoate, D,L-3-hydroxybutanoate, citrate, maleate, succinate, L-tartrate, L-threonine, L-serine, L-hydroxymalonate, D-glutamate, 2-oxocaproate, 2-oxoisovalerate, glyoxylate, 2-oxoglutarate, 2-oxobutanoate
-
-
?
additional information
?
-
-
no substrate: pyruvate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52
-
pH 7.6, reduction of oxaloacetate, cosubstrate NADP+
60
-
pH 7.6, reduction of oxaloacetate, cosubstrate NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). MDH_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
308
0
33490
Swiss-Prot
-
MDH_METKA
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
317
0
34609
Swiss-Prot
-
MDH_METMP
Methanococcus maripaludis (strain S2 / LL)
314
0
34468
Swiss-Prot
-
MDH_METST
Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)
317
0
34857
Swiss-Prot
-
MDH_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
325
0
35933
Swiss-Prot
-
MDH_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
325
0
35860
Swiss-Prot
-
A0A7T1FRI9_PROCL
332
1
35862
TrEMBL
other Location (Reliability: 4)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
124000
-
size exclusion chromatography-multi angle laser light scattering
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme, sitting drop vapor diffusion method, using 10% (w/v) PEG 6000 and 100 mM EPES at pH 7.0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oikawa, T.; Yamamoto, N.; Shimoke, K.; Uesato, S.; Ikeuchi, T.; Fujioka, T.
Purification, characterization, and overexpression of psychrophilic and thermolabile malate dehydrogenase of a novel antarctic psychrotolerant, Flavobacterium frigidimaris KUC-1
Biosci. Biotechnol. Biochem.
69
2146-2154
2005
Flavobacterium frigidimaris, Flavobacterium frigidimaris KUC-1
brenda
Thompson, H.; Tersteegen, A.; Thauer, R.; Hedderich, R.
Two malate dehydrogenases in Methanobacterium thermoautotrophicum
Arch. Microbiol.
170
38-42
1998
Methanothermobacter thermautotrophicus
brenda
Roche, J.; Girard, E.; Mas, C.; Madern, D.
The archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization
J. Struct. Biol.
208
7-17
2019
Ignicoccus islandicus
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.1.299)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
About BRENDA
Help
Download
Contribution
member of
curated at
curated at
Server: brenda3 Ver: 69ad221-main (2022-06-24 14:26:09 +0200)